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{{Short description|Species of archaeon}}
{{Short description|Species of archaeon}}
{{Cleanup|date=September 2023|reason=grammar and formatting issues scattered throughout}}
{{Italic title}}
{{Italic title}}
{{Taxobox
{{Taxobox
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| ordo = [[Sulfolobales]]
| ordo = [[Sulfolobales]]
| familia = [[Sulfolobaceae]]
| familia = [[Sulfolobaceae]]
| genus = ''[[Saccharolobus]]''
| genus = ''[[Sulfolobus]]''
| species = '''''S. solfataricus'''''
| species = '''''S. solfataricus'''''
| binomial = '''''Saccharolobus solfataricus'''''
| binomial = '''''Sulfolobus solfataricus'''''
| binomial_authority = (Stetter and Zillig 1980) Sakai and Kurosawa 2018
| binomial_authority = Zillig et al. 1980
| synonyms =
* ''Saccharolobus solfataricus'' <small>(Zillig et al. 1980) Sakai & Kurosawa 2018</small>
}}
}}


'''''Saccharolobus solfataricus''''' is a [[species]] of [[thermophilic]] [[archaeon]]. It was transferred from the genus ''Sulfolobus'' to the new genus ''Saccharolobus'' with the description of Saccharolobus caldissimus in 2018.<ref name="Sakai_2018">{{cite journal | vauthors = Sakai HD, Kurosawa N | title = Saccharolobus caldissimus gen. nov., sp. nov., a facultatively anaerobic iron-reducing hyperthermophilic archaeon isolated from an acidic terrestrial hot spring, and reclassification of Sulfolobus solfataricus as Saccharolobus solfataricus comb. nov. and Sulfolobus shibatae as Saccharolobus shibatae comb. nov | journal = International Journal of Systematic and Evolutionary Microbiology | volume = 68 | issue = 4 | pages = 1271–1278 | date = April 2018 | pmid = 29485400 | doi = 10.1099/ijsem.0.002665 | s2cid = 4528286 | doi-access = free }}</ref>
'''''Saccharolobus solfataricus''''' is a [[species]] of [[thermophilic]] [[archaeon]]. It was transferred from the genus ''Sulfolobus'' to the new genus ''Saccharolobus'' with the description of ''Saccharolobus caldissimus'' in 2018.<ref name="Sakai_2018">{{cite journal | vauthors = Sakai HD, Kurosawa N | title = Saccharolobus caldissimus gen. nov., sp. nov., a facultatively anaerobic iron-reducing hyperthermophilic archaeon isolated from an acidic terrestrial hot spring, and reclassification of Sulfolobus solfataricus as Saccharolobus solfataricus comb. nov. and Sulfolobus shibatae as Saccharolobus shibatae comb. nov | journal = International Journal of Systematic and Evolutionary Microbiology | volume = 68 | issue = 4 | pages = 1271–1278 | date = April 2018 | pmid = 29485400 | doi = 10.1099/ijsem.0.002665 | s2cid = 4528286 | doi-access = free }}</ref>


It was first isolated and discovered in the [[Solfatara (volcano)|Solfatara]] volcano (which it was subsequently named after) in 1980 by two Germans microbiologists Karl Setter and Wolfram Zillig, in Solfatara volcano (Pisciarelli-Campania, Italy).<ref>{{cite web|url=http://intercept.cnrs.fr/where-was-sulfolobus-solfataricus-first-found/|title=Where was Sulfolobus solfataricus first found?|website=www.intercept.cnrs.fr|date=15 January 2019}}</ref>
It was first discovered and isolated from the [[Solfatara (volcano)|Solfatara]] volcano (Pisciarelli-Campania, Italy) in 1980 by two German microbiologists Karl Setter and Wolfram Zillig.<ref>{{cite web |date=15 January 2019 |title=Where was Sulfolobus solfataricus first found? |url=http://intercept.cnrs.fr/where-was-sulfolobus-solfataricus-first-found/ |website=www.intercept.cnrs.fr}}</ref>


However, these organisms are not isolated to volcanoes but are found all over the world in places such as hot springs. The species grows best in temperatures around 80° Celsius, a pH level between 2 and 4, and enough sulfur for ''solfataricus'' to metabolize in order to gain energy. These conditions qualify it as an [[extremophile]] and it is specifically known as a [[thermoacidophile]] because of its preference to high temperatures and low pH levels and it is also in aerobic and heterotropic categories for its metabolic system.<ref name="Molecular biology of extremophiles">{{cite journal | vauthors = Ciaramella M, Pisani FM, Rossi M | title = Molecular biology of extremophiles: recent progress on the hyperthermophilic archaeon Sulfolobus | journal = Antonie van Leeuwenhoek | volume = 81 | issue = 1–4 | pages = 85–97 | date = August 2002 | pmid = 12448708 | doi = 10.1023/A:1020577510469 | s2cid = 8330296 }}</ref> It usually has a spherical cell shape and it makes frequent lobes. Being an [[autotroph]] it receives energy from growing on sulfur or even a variety of organic compounds.<ref name="pmid4559703">{{cite journal | vauthors = Brock TD, Brock KM, Belly RT, Weiss RL | title = Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature | journal = Archiv für Mikrobiologie| volume = 84 | issue = 1 | pages = 54–68 | date = 1972 | pmid = 4559703 | doi = 10.1007/bf00408082 | s2cid = 9204044 }}</ref>
However, these organisms are not isolated to volcanoes but are found all over the world in places such as hot springs. The species grows best in temperatures around 80 °C, a pH level between 2 and 4, and with enough sulfur for ''S.'' ''solfataricus'' to metabolize in order to gain energy. These conditions qualify it as an [[extremophile]] and it is specifically known as a [[thermoacidophile]] because of its preference for high temperatures and low pH levels. It is also aerobic and heterotropic due to its metabolic system.<ref name="Molecular biology of extremophiles">{{cite journal | vauthors = Ciaramella M, Pisani FM, Rossi M | title = Molecular biology of extremophiles: recent progress on the hyperthermophilic archaeon Sulfolobus | journal = Antonie van Leeuwenhoek | volume = 81 | issue = 1–4 | pages = 85–97 | date = August 2002 | pmid = 12448708 | doi = 10.1023/A:1020577510469 | s2cid = 8330296 }}</ref> Being an [[autotroph]], it receives energy by growing on sulfur or even a variety of organic compounds.<ref name="pmid4559703">{{cite journal | vauthors = Brock TD, Brock KM, Belly RT, Weiss RL | title = Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature | journal = Archiv für Mikrobiologie| volume = 84 | issue = 1 | pages = 54–68 | date = 1972 | pmid = 4559703 | doi = 10.1007/bf00408082 | s2cid = 9204044 }}</ref> It usually has a spherical cell shape and it makes frequent lobes. <!-- Inserting an image of this organism may be helpful. -->


Currently, it is the most widely studied organism that is within the [[Thermoproteota]] branch. ''Solfataricus'' are researched for their methods of DNA replication, cell cycle, chromosomal integration, transcription, RNA processing, and translation. All the data points to the organism having a large percent of archaeal-specific genes, which showcases the differences between the three types of microbes: [[archaea]], [[bacteria]], and [[eukarya]].
Currently, it is the most widely studied organism within the [[Thermoproteota]] branch. ''Solfataricus'' are examined for their methods of DNA replication, cell cycle, chromosomal integration, transcription, RNA processing, and translation. All of the data points to the organism having a large percent of archaeal-specific genes, which shows the differences between the three types of microbes: [[archaea]], [[bacteria]], and [[eukaryote]].


== Genome ==
== Genome ==
''Sulfolobus solfataricus'' is the most studied [[microorganism]] from a molecular, genetic and biochemical point of view for its ability to thrive in extreme environments; it is easily cultivable in laboratory; moreover, it can exchange genetic material through processes of transformation, transduction and conjugation.
''Sulfolobus solfataricus'' is the most studied [[microorganism]] from a molecular, genetic, and biochemical point of view for its ability to thrive in extreme environments. It can grow easily in the laboratory; moreover, it can exchange genetic material through processes of transformation, transduction. and conjugation.


The major motivation for sequencing these microorganisms is because of the [[thermostability]] of [[protein]]s that normally denature at high [[temperature]]. The complete sequence the [[genome]] of ''S. solfataricus'' was completed in 2001.<ref>{{cite journal | vauthors = Charlebois RL, Gaasterland T, Ragan MA, Doolittle WF, Sensen CW | title = The Sulfolobus solfataricus P2 genome project | journal = FEBS Letters | volume = 389 | issue = 1 | pages = 88–91 | date = June 1996 | pmid = 8682213 | doi = 10.1016/s0014-5793(97)81281-1 | s2cid = 221414122 }}</ref> On a single chromosome, there are 2,992,245 base pairs which encode for 2,977 [[protein]]s and copious RNAs. One-third of ''S. solfataricus'' encoded proteins have no homologs in other genomes. For the remaining encoded proteins, 40% are specific to [[Archaea]], 12% are shared with [[Bacteria]], and 2.3% are shared with [[Eukarya]].;<ref name="She_2001" /> 33% of these proteins is encoded exclusively in ''Sulfolobus''. A high number of ORFs ([[open reading frame]]) are highly similar in ''Thermoplasma''.<ref name="Molecular biology of extremophiles"/>
The major motivation for sequencing these microorganisms is the [[thermostability]] of [[protein]]s that normally denature at a high [[temperature]]. The complete sequence the [[genome]] of ''S. solfataricus'' was completed in 2001.<ref>{{cite journal | vauthors = Charlebois RL, Gaasterland T, Ragan MA, Doolittle WF, Sensen CW | title = The Sulfolobus solfataricus P2 genome project | journal = FEBS Letters | volume = 389 | issue = 1 | pages = 88–91 | date = June 1996 | pmid = 8682213 | doi = 10.1016/s0014-5793(97)81281-1 | s2cid = 221414122 }}</ref> On a single chromosome, there are 2,992,245 base pairs which encode for 2,977 [[protein]]s and copious RNAs. One-third of ''S. solfataricus'' encoded proteins have no homologs in other genomes. For the remaining encoded proteins, 40% are specific to [[Archaea]], 12% are shared with [[Bacteria]], and 2.3% are shared with [[Eukaryote]];<ref name="She_2001" /> 33% of these proteins are encoded exclusively in ''Sulfolobus''. A high number of [[open reading frame]]<nowiki/>s (ORFs) are highly similar in ''Thermoplasma''.<ref name="Molecular biology of extremophiles"/>


[[Small nucleolar RNA SNORD116|Small nucleolar RNAs]] (snoRNAs), already present in eukaryotes, have also been identified in ''S.Solfataricus'' and ''S.acidolcaldarius''. They are already known for the role they play in posttranscriptional modifications and removal of [[intron]]s from ribosomal RNA in Eucarya.<ref>{{cite journal | vauthors = Omer AD, Lowe TM, Russell AG, Ebhardt H, Eddy SR, Dennis PP | title = Homologs of small nucleolar RNAs in Archaea | journal = Science | volume = 288 | issue = 5465 | pages = 517–22 | date = April 2000 | pmid = 10775111 | doi = 10.1126/science.288.5465.517 | url = https://semanticscholar.org/paper/2a65285f4fb55f59396a9a577da81f327b3e3cc7 | bibcode = 2000Sci...288..517O | s2cid = 15552500 }}</ref>
[[Small nucleolar RNA SNORD116|Small nucleolar RNAs]] (snoRNAs), already present in eukaryotes, have also been identified in ''S. solfataricus'' and ''S. acidolcaldarius''. They are already known for the role they play in post-transcriptional modifications and removal of [[intron]]s from ribosomal RNA in [[Eukaryote]].<ref>{{cite journal | vauthors = Omer AD, Lowe TM, Russell AG, Ebhardt H, Eddy SR, Dennis PP | title = Homologs of small nucleolar RNAs in Archaea | journal = Science | volume = 288 | issue = 5465 | pages = 517–22 | date = April 2000 | pmid = 10775111 | doi = 10.1126/science.288.5465.517 | bibcode = 2000Sci...288..517O | s2cid = 15552500 }}</ref>


The genome of ''Sulfolobus'' is characterised by the presence of short tandem repeats, insertion and repetitive elements, it has a wide range of diversity as it has 200 different ISs insertion sequence elements.
The genome of ''Sulfolobus'' is characterized by the presence of short tandem repeats, insertion and repetitive elements. It has a wide range of diversity with 200 different insertion sequence elements.


=== Thermophilic reverse gyrase ===
=== Thermophilic reverse gyrase ===
The stabilisation of the double helix against denaturation, in the Archaea, is due to the presence of a particular specific thermophilic [[enzyme]], reverse gyrase. It was discovered in hyperthermophilic and thermophilic Archaea and Bacteria. There are two [[gene]]s in ''Sulfolobus'' that each encode a reverse gyrase.<ref>{{cite journal | vauthors = Couturier M, Bizard AH, Garnier F, Nadal M | title = Insight into the cellular involvement of the two reverse gyrases from the hyperthermophilic archaeon Sulfolobus solfataricus | journal = BMC Molecular Biology | volume = 15 | issue = 1 | pages = 18 | date = September 2014 | pmid = 25200003 | pmc = 4183072 | doi = 10.1186/1471-2199-15-18 }}</ref> It is defined atypical Dna [[topoisomerase]]s and the basic activity consists in the production of positive supercoils in a closed circular Dna. Positive supercoiling is important to prevent the formation of open complexes. Reverse gyrases are composed of two domains: the first one is the [[helicase]] like and second one is the topoisomerase I. A possible role of reverse gyrase could be the use of positive supercoiling to assemble chromatin-like structures.<ref>{{cite journal | vauthors = Déclais AC, Marsault J, Confalonieri F, de La Tour CB, Duguet M | title = Reverse gyrase, the two domains intimately cooperate to promote positive supercoiling | journal = The Journal of Biological Chemistry | volume = 275 | issue = 26 | pages = 19498–504 | date = June 2000 | pmid = 10748189 | doi = 10.1074/jbc.m910091199 | doi-access = free }}</ref> In 1997 scientists discovered another important feature of ''Sulfolobus'': this microorganism contains a type-II topoisomerase, called TopoVI, whose A subunit is homologous to the [[Meiosis|meiotic]] recombination factor, [[Spo11]] which plays a predominant role initiation of meiotic recombination in all Eucarya.<ref>{{cite journal | vauthors = Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, Forterre P | title = An atypical topoisomerase II from Archaea with implications for meiotic recombination | journal = Nature | volume = 386 | issue = 6623 | pages = 414–7 | date = March 1997 | pmid = 9121560 | doi = 10.1038/386414a0 | bibcode = 1997Natur.386..414B | s2cid = 4327493 }}</ref><ref>{{cite journal | vauthors = Forterre P, Bergerat A, Lopez-Garcia P | title = The unique DNA topology and DNA topoisomerases of hyperthermophilic archaea | journal = FEMS Microbiology Reviews | volume = 18 | issue = 2–3 | pages = 237–48 | date = May 1996 | pmid = 8639331 | doi = 10.1111/j.1574-6976.1996.tb00240.x | doi-access = free }}</ref>
The stabilization of the double helix<!-- Is this DNA? --> against denaturation, in the Archaea, is due to the presence of a particular thermophilic [[enzyme]], reverse gyrase. It was discovered in hyper-thermophilic and thermophilic Archaea and Bacteria. There are two [[gene]]s in ''Sulfolobus'' that each encode a reverse gyrase.<ref>{{cite journal | vauthors = Couturier M, Bizard AH, Garnier F, Nadal M | title = Insight into the cellular involvement of the two reverse gyrases from the hyperthermophilic archaeon Sulfolobus solfataricus | journal = BMC Molecular Biology | volume = 15 | issue = 1 | pages = 18 | date = September 2014 | pmid = 25200003 | pmc = 4183072 | doi = 10.1186/1471-2199-15-18 | doi-access = free }}</ref> It is defined as an atypical DNA [[topoisomerase]] and the basic activity consists of the production of positive supercoils in a closed circular DNA. Positive supercoiling is important to prevent the formation of open complexes. Reverse gyrases are composed of two domains: the first one is the [[helicase]] and second one is the topoisomerase I. A possible role of reverse gyrase could be the use of positive supercoiling to assemble chromatin-like structures.<ref>{{cite journal | vauthors = Déclais AC, Marsault J, Confalonieri F, de La Tour CB, Duguet M | title = Reverse gyrase, the two domains intimately cooperate to promote positive supercoiling | journal = The Journal of Biological Chemistry | volume = 275 | issue = 26 | pages = 19498–504 | date = June 2000 | pmid = 10748189 | doi = 10.1074/jbc.m910091199 | doi-access = free }}</ref> In 1997, scientists discovered another important feature of ''Sulfolobus'': a type-II topoisomerase, called TopoVI, whose A subunit is homologous to the [[Meiosis|meiotic]] recombination factor, [[Spo11]], which plays a predominant role in the initiation of meiotic recombination in all Eukaryotes.<ref>{{cite journal | vauthors = Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, Forterre P | title = An atypical topoisomerase II from Archaea with implications for meiotic recombination | journal = Nature | volume = 386 | issue = 6623 | pages = 414–7 | date = March 1997 | pmid = 9121560 | doi = 10.1038/386414a0 | bibcode = 1997Natur.386..414B | s2cid = 4327493 }}</ref><ref>{{cite journal | vauthors = Forterre P, Bergerat A, Lopez-Garcia P | title = The unique DNA topology and DNA topoisomerases of hyperthermophilic archaea | journal = FEMS Microbiology Reviews | volume = 18 | issue = 2–3 | pages = 237–48 | date = May 1996 | pmid = 8639331 | doi = 10.1111/j.1574-6976.1996.tb00240.x | doi-access = free }}</ref>


''S. solfataricus'' is composed of three topoisomerases of type I, TopA and two reverse gyrases, TopR1 and TopR2, and one topoisomerase of type II, TopoVI.<ref>{{cite journal | vauthors = Couturier M, Gadelle D, Forterre P, Nadal M, Garnier F | title = The reverse gyrase TopR1 is responsible for the homeostatic control of DNA supercoiling in the hyperthermophilic archaeon Sulfolobus solfataricus | journal = Molecular Microbiology | date = November 2019 | volume = 113 | issue = 2 | pages = 356–368 | pmid = 31713907 | doi = 10.1111/mmi.14424 | s2cid = 207945754 }}</ref>
''S. solfataricus'' is composed of three topoisomerases of type I, TopA and two reverse gyrases, TopR1 and TopR2, and one topoisomerase of type II, TopoVI.<ref>{{cite journal | vauthors = Couturier M, Gadelle D, Forterre P, Nadal M, Garnier F | title = The reverse gyrase TopR1 is responsible for the homeostatic control of DNA supercoiling in the hyperthermophilic archaeon Sulfolobus solfataricus | journal = Molecular Microbiology | date = November 2019 | volume = 113 | issue = 2 | pages = 356–368 | pmid = 31713907 | doi = 10.1111/mmi.14424 | s2cid = 207945754 | doi-access = free }}</ref>


=== Dna binding proteins ===
=== DNA binding proteins ===
In the Phylum Thermoproteota there are three proteins that bind the minor groove of [[DNA|Dna]] like [[histone]]s:Alba, Cren7, and Sso7d, that are modified after the translation process. These are small and have been found in several strains of Sulfolobus but not in other genome. Chromatin protein in ''Sulfolobus'' represent 1-5% of the total. They can have both structural and regulatory functions. These look like human HMG-box proteins, because of their influence on genomes, for the expression and the stability, and on epigenetic processes.<ref>{{cite journal | vauthors = Malarkey CS, Churchill ME | title = The high mobility group box: the ultimate utility player of a cell | journal = Trends in Biochemical Sciences | volume = 37 | issue = 12 | pages = 553–62 | date = December 2012 | pmid = 23153957 | pmc = 4437563 | doi = 10.1016/j.tibs.2012.09.003 }}</ref> In species lacking histones they can be acetylated and methylated like eukaryotic histones.<ref>{{cite journal | vauthors = Payne S, McCarthy S, Johnson T, North E, Blum P | title = Sulfolobus solfataricus | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 115 | issue = 48 | pages = 12271–12276 | date = November 2018 | pmid = 30425171 | pmc = 6275508 | doi = 10.1073/pnas.1808221115 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Guagliardi A, Cerchia L, Moracci M, Rossi M | title = The chromosomal protein sso7d of the crenarchaeon ''Sulfolobus solfataricus'' rescues aggregated proteins in an ATP hydrolysis-dependent manner | journal = The Journal of Biological Chemistry | volume = 275 | issue = 41 | pages = 31813–8 | date = October 2000 | pmid = 10908560 | doi = 10.1074/jbc.m002122200 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Shehi E, Granata V, Del Vecchio P, Barone G, Fusi P, Tortora P, Graziano G | title = Thermal stability and DNA binding activity of a variant form of the Sso7d protein from the archeon ''Sulfolobus solfataricus'' truncated at leucine 54 | journal = Biochemistry | volume = 42 | issue = 27 | pages = 8362–8 | date = July 2003 | pmid = 12846585 | doi = 10.1021/bi034520t }}</ref><ref>{{cite journal | vauthors = Baumann H, Knapp S, Karshikoff A, Ladenstein R, Härd T | title = DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus | journal = Journal of Molecular Biology | volume = 247 | issue = 5 | pages = 840–6 | date = April 1995 | pmid = 7723036 | doi = 10.1006/jmbi.1995.0184 }}</ref> ''Sulfolobus'' strains present different peculiar DNA binding proteins, such as the Sso7d protein family. They stabilize the double helix, preventing [[Denaturation (biochemistry)|denaturation]] at high temperature thus promoting annealing above the [[melting point]].<ref>{{cite journal | vauthors = Guagliardi A, Napoli A, Rossi M, Ciaramella M | title = Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein | journal = Journal of Molecular Biology | volume = 267 | issue = 4 | pages = 841–8 | date = April 1997 | pmid = 9135116 | doi = 10.1006/jmbi.1996.0873 }}</ref>
In the phylum Thermoproteota, there are three proteins that bind to the minor groove of [[DNA]]-like [[histone]]s, Alba, Cren7, and Sso7d, that are modified after the translation process. These histones are small and have been found in several strains of ''Sulfolobus'' but not in other genomes. Chromatin protein in ''Sulfolobus'' represent 1-5% of the total genome. They can have both structural and regulatory functions. These look like human HMG-box proteins, because of their influence on genomes, expression and stability, and epigenetic processes.<ref>{{cite journal | vauthors = Malarkey CS, Churchill ME | title = The high mobility group box: the ultimate utility player of a cell | journal = Trends in Biochemical Sciences | volume = 37 | issue = 12 | pages = 553–62 | date = December 2012 | pmid = 23153957 | pmc = 4437563 | doi = 10.1016/j.tibs.2012.09.003 }}</ref> <!-- Is HMG "high mobility group"? Consider adding the definition of this term. -->In species lacking histones, they can be acetylated and methylated like eukaryotic histones.<ref>{{cite journal | vauthors = Payne S, McCarthy S, Johnson T, North E, Blum P | title = Sulfolobus solfataricus | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 115 | issue = 48 | pages = 12271–12276 | date = November 2018 | pmid = 30425171 | pmc = 6275508 | doi = 10.1073/pnas.1808221115 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Guagliardi A, Cerchia L, Moracci M, Rossi M | title = The chromosomal protein sso7d of the crenarchaeon ''Sulfolobus solfataricus'' rescues aggregated proteins in an ATP hydrolysis-dependent manner | journal = The Journal of Biological Chemistry | volume = 275 | issue = 41 | pages = 31813–8 | date = October 2000 | pmid = 10908560 | doi = 10.1074/jbc.m002122200 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Shehi E, Granata V, Del Vecchio P, Barone G, Fusi P, Tortora P, Graziano G | title = Thermal stability and DNA binding activity of a variant form of the Sso7d protein from the archeon ''Sulfolobus solfataricus'' truncated at leucine 54 | journal = Biochemistry | volume = 42 | issue = 27 | pages = 8362–8 | date = July 2003 | pmid = 12846585 | doi = 10.1021/bi034520t }}</ref><ref>{{cite journal | vauthors = Baumann H, Knapp S, Karshikoff A, Ladenstein R, Härd T | title = DNA-binding surface of the Sso7d protein from Sulfolobus solfataricus | journal = Journal of Molecular Biology | volume = 247 | issue = 5 | pages = 840–6 | date = April 1995 | pmid = 7723036 | doi = 10.1006/jmbi.1995.0184 | doi-access = free }}</ref> ''Sulfolobus'' strains present different peculiar DNA binding proteins, such as the Sso7d protein family. They stabilize the double helix, preventing [[Denaturation (biochemistry)|denaturation]] at high temperature and thus promoting annealing above the [[melting point]].<ref>{{cite journal | vauthors = Guagliardi A, Napoli A, Rossi M, Ciaramella M | title = Annealing of complementary DNA strands above the melting point of the duplex promoted by an archaeal protein | journal = Journal of Molecular Biology | volume = 267 | issue = 4 | pages = 841–8 | date = April 1997 | pmid = 9135116 | doi = 10.1006/jmbi.1996.0873 }}</ref> <!-- What is the melting point? -->


The major component of archael chromatin is represented by Sac10b family protein known as Alba (Acetylation lowers binding affinity).<ref>{{cite journal | vauthors = Forterre P, Confalonieri F, Knapp S | title = Identification of the gene encoding archeal-specific DNA-binding proteins of the Sac10b family | journal = Molecular Microbiology | volume = 32 | issue = 3 | pages = 669–70 | date = May 1999 | pmid = 10320587 | doi = 10.1046/j.1365-2958.1999.01366.x | s2cid = 28146814 }}</ref><ref>{{cite journal | vauthors = Xue H, Guo R, Wen Y, Liu D, Huang L | title = An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion | journal = Journal of Bacteriology | volume = 182 | issue = 14 | pages = 3929–33 | date = July 2000 | pmid = 10869069 | pmc = 94576 | doi = 10.1128/JB.182.14.3929-3933.2000 }}</ref> These proteins are small, basic and dimeric nucleic acid-binding proteins. Furthermore, it is conserved in most sequenced archeal genomes.<ref>{{cite journal | vauthors = Goyal M, Banerjee C, Nag S, Bandyopadhyay U | title = The Alba protein family: Structure and function | journal = Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | volume = 1864 | issue = 5 | pages = 570–83 | date = May 2016 | pmid = 26900088 | doi = 10.1016/j.bbapap.2016.02.015 }}</ref><ref>{{cite journal | vauthors = Wardleworth BN, Russell RJ, Bell SD, Taylor GL, White MF | title = Structure of Alba: an archaeal chromatin protein modulated by acetylation | journal = The EMBO Journal | volume = 21 | issue = 17 | pages = 4654–62 | date = September 2002 | pmid = 12198167 | pmc = 125410 | doi = 10.1093/emboj/cdf465 }}</ref> The acetylation state of Alba, as an example, affects promoter access and transcription in vitro, whereas the methylation state of another ''Sulfolobus'' chromatin protein, Sso7D, is altered by culture temperature.<ref>{{cite journal | vauthors = Bell SD, Botting CH, Wardleworth BN, Jackson SP, White MF | title = The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation | journal = Science | volume = 296 | issue = 5565 | pages = 148–51 | date = April 2002 | pmid = 11935028 | doi = 10.1126/science.1070506 | bibcode = 2002Sci...296..148B | s2cid = 27858056 | url = https://semanticscholar.org/paper/849e4bea494353d2b417fab2707783b0dfd2dbf6 }}</ref><ref>{{cite journal | vauthors = Baumann H, Knapp S, Lundbäck T, Ladenstein R, Härd T | title = Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus | journal = Nature Structural Biology | volume = 1 | issue = 11 | pages = 808–19 | date = November 1994 | pmid = 7634092 | doi = 10.1038/nsb1194-808 | s2cid = 37220619 }}</ref>
The major component of Archaea chromatin is represented by Sac10b family protein known as Alba (acetylation lowers binding affinity).<ref>{{cite journal | vauthors = Forterre P, Confalonieri F, Knapp S | title = Identification of the gene encoding archeal-specific DNA-binding proteins of the Sac10b family | journal = Molecular Microbiology | volume = 32 | issue = 3 | pages = 669–70 | date = May 1999 | pmid = 10320587 | doi = 10.1046/j.1365-2958.1999.01366.x | s2cid = 28146814 }}</ref><ref>{{cite journal | vauthors = Xue H, Guo R, Wen Y, Liu D, Huang L | title = An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion | journal = Journal of Bacteriology | volume = 182 | issue = 14 | pages = 3929–33 | date = July 2000 | pmid = 10869069 | pmc = 94576 | doi = 10.1128/JB.182.14.3929-3933.2000 }}</ref> These proteins are small, basic, and dimeric nucleic acid-binding proteins. Furthermore, it is conserved in most sequenced Archaea genomes.<ref>{{cite journal | vauthors = Goyal M, Banerjee C, Nag S, Bandyopadhyay U | title = The Alba protein family: Structure and function | journal = Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | volume = 1864 | issue = 5 | pages = 570–83 | date = May 2016 | pmid = 26900088 | doi = 10.1016/j.bbapap.2016.02.015 }}</ref><ref>{{cite journal | vauthors = Wardleworth BN, Russell RJ, Bell SD, Taylor GL, White MF | title = Structure of Alba: an archaeal chromatin protein modulated by acetylation | journal = The EMBO Journal | volume = 21 | issue = 17 | pages = 4654–62 | date = September 2002 | pmid = 12198167 | pmc = 125410 | doi = 10.1093/emboj/cdf465 }}</ref> The acetylation state of Alba affects promoter access and transcription in vitro, whereas the methylation state of another ''Sulfolobus'' chromatin protein, Sso7D, is altered by culture temperature.<ref>{{cite journal | vauthors = Bell SD, Botting CH, Wardleworth BN, Jackson SP, White MF | title = The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation | journal = Science | volume = 296 | issue = 5565 | pages = 148–51 | date = April 2002 | pmid = 11935028 | doi = 10.1126/science.1070506 | bibcode = 2002Sci...296..148B | s2cid = 27858056 }}</ref><ref>{{cite journal | vauthors = Baumann H, Knapp S, Lundbäck T, Ladenstein R, Härd T | title = Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus | journal = Nature Structural Biology | volume = 1 | issue = 11 | pages = 808–19 | date = November 1994 | pmid = 7634092 | doi = 10.1038/nsb1194-808 | s2cid = 37220619 }}</ref>


The work of Wolfram Zillig's group, representing early evidence of the eukaryotic characteristics of the transcription in Archea, has since made ''Sulfolobus'' an ideal model system for transcription studies. Recent studies in Sulfolobus, in addition to other archaeal species, mainly focus on the composition, function and regulation of the transcription machinery in these organisms and on fundamental conserved aspects of this process in both Eucarya and Archaea.<ref>{{cite journal | vauthors = Zillig W, Stetter KO, Janeković D | title = DNA-dependent RNA polymerase from the archaebacterium Sulfolobus acidocaldarius | journal = European Journal of Biochemistry | volume = 96 | issue = 3 | pages = 597–604 | date = June 1979 | pmid = 380989 | doi = 10.1111/j.1432-1033.1979.tb13074.x | doi-access = free }}</ref>
The work of Wolfram Zillig's group, representing early evidence of the eukaryotic characteristics of transcription in Archaea, has since made ''Sulfolobus'' an ideal model system for transcription studies. Recent studies in ''Sulfolobus'', in addition to other Archaea species, mainly focus on the composition, function, and regulation of the transcription machinery and on fundamental conserved aspects of this process in both Eukaryotes and Archaea.<ref>{{cite journal | vauthors = Zillig W, Stetter KO, Janeković D | title = DNA-dependent RNA polymerase from the archaebacterium Sulfolobus acidocaldarius | journal = European Journal of Biochemistry | volume = 96 | issue = 3 | pages = 597–604 | date = June 1979 | pmid = 380989 | doi = 10.1111/j.1432-1033.1979.tb13074.x | doi-access = free }}</ref>


==DNA transfer==
==DNA transfer==
Exposure of ''Saccharolobus solfataricus'' to the DNA damaging agents [[Ultraviolet|UV-irradiation]], [[bleomycin]] or [[Mitomycins|mitomycin C]] induces cellular aggregation.<ref name="Frols">{{cite journal | vauthors = Fröls S, Ajon M, Wagner M, Teichmann D, Zolghadr B, Folea M, Boekema EJ, Driessen AJ, Schleper C, Albers SV | display-authors = 6 | title = UV-inducible cellular aggregation of the hyperthermophilic archaeon Sulfolobus solfataricus is mediated by pili formation | journal = Molecular Microbiology | volume = 70 | issue = 4 | pages = 938–52 | date = November 2008 | pmid = 18990182 | doi = 10.1111/j.1365-2958.2008.06459.x | url = https://pure.rug.nl/ws/files/56956856/UV_inducible_cellular_aggregation_of_the_hyperthermophilic_archaeon_Sulfolobus_solfataricus_is_mediated_by_pili_formation.pdf | doi-access = free }}</ref> Other physical stressors, such as changes in pH or temperature shift, do not induce aggregation, suggesting that induction of aggregation is caused specifically by DNA damage. Ajon et al.<ref name="Ajon">{{cite journal | vauthors = Ajon M, Fröls S, van Wolferen M, Stoecker K, Teichmann D, Driessen AJ, Grogan DW, Albers SV, Schleper C | display-authors = 6 | title = UV-inducible DNA exchange in hyperthermophilic archaea mediated by type IV pili | journal = Molecular Microbiology | volume = 82 | issue = 4 | pages = 807–17 | date = November 2011 | pmid = 21999488 | doi = 10.1111/j.1365-2958.2011.07861.x | url = https://pure.rug.nl/ws/files/6771142/2011MolMicrobiolAjon.pdf | doi-access = free }}</ref> showed that UV-induced cellular aggregation mediates chromosomal marker exchange with high frequency. Recombination rates exceeded those of uninduced cultures by up to three orders of magnitude. Frols et al.<ref name="Frols" /><ref name="pmid19143598">{{cite journal | vauthors = Fröls S, White MF, Schleper C | title = Reactions to UV damage in the model archaeon Sulfolobus solfataricus | journal = Biochemical Society Transactions | volume = 37 | issue = Pt 1 | pages = 36–41 | date = February 2009 | pmid = 19143598 | doi = 10.1042/BST0370036 | s2cid = 837167 | url = https://semanticscholar.org/paper/9f9e4150bf0567070d4ba5ea11ef2615325a8120 }}</ref> and Ajon et al.<ref name="Ajon" /> hypothesized that the UV-inducible DNA transfer process and subsequent [[homologous recombination]]al repair represents an important mechanism to maintain chromosome integrity. This response may be a primitive form of sexual interaction, similar to the more well-studied bacterial transformation that is also associated with DNA transfer between cells leading to homologous recombinational repair of DNA damage.{{Citation needed|date=December 2019|reason=removed citation to predatory publisher content}}
Exposure of ''Saccharolobus solfataricus'' to the DNA damaging agents, ultraviolet ([[Ultraviolet|UV) irradiation]], [[bleomycin]], or [[Mitomycins|mitomycin C]], induces cellular aggregation.<ref name="Frols">{{cite journal | vauthors = Fröls S, Ajon M, Wagner M, Teichmann D, Zolghadr B, Folea M, Boekema EJ, Driessen AJ, Schleper C, Albers SV | display-authors = 6 | title = UV-inducible cellular aggregation of the hyperthermophilic archaeon Sulfolobus solfataricus is mediated by pili formation | journal = Molecular Microbiology | volume = 70 | issue = 4 | pages = 938–52 | date = November 2008 | pmid = 18990182 | doi = 10.1111/j.1365-2958.2008.06459.x | url = https://pure.rug.nl/ws/files/56956856/UV_inducible_cellular_aggregation_of_the_hyperthermophilic_archaeon_Sulfolobus_solfataricus_is_mediated_by_pili_formation.pdf | doi-access = free }}</ref> <!-- Consider describing "aggregation". -->Other physical stressors, such as changes in pH or temperature shift, do not induce aggregation, suggesting that the induction of aggregation is caused specifically by DNA damage. Ajon et al.<ref name="Ajon">{{cite journal | vauthors = Ajon M, Fröls S, van Wolferen M, Stoecker K, Teichmann D, Driessen AJ, Grogan DW, Albers SV, Schleper C | display-authors = 6 | title = UV-inducible DNA exchange in hyperthermophilic archaea mediated by type IV pili | journal = Molecular Microbiology | volume = 82 | issue = 4 | pages = 807–17 | date = November 2011 | pmid = 21999488 | doi = 10.1111/j.1365-2958.2011.07861.x | url = https://pure.rug.nl/ws/files/6771142/2011MolMicrobiolAjon.pdf | doi-access = free }}</ref> showed that UV-induced cellular aggregation mediates chromosomal marker exchange with high frequency. Recombination rates exceeded those of uninduced cultures by up to three orders of magnitude. Frols et al.<ref name="Frols" /><ref name="pmid19143598">{{cite journal | vauthors = Fröls S, White MF, Schleper C | title = Reactions to UV damage in the model archaeon Sulfolobus solfataricus | journal = Biochemical Society Transactions | volume = 37 | issue = Pt 1 | pages = 36–41 | date = February 2009 | pmid = 19143598 | doi = 10.1042/BST0370036 | s2cid = 837167 }}</ref> and Ajon et al.<ref name="Ajon" /> hypothesized that the UV-induced DNA transfer process and subsequent [[homologous recombination]]al repair represents an important mechanism to maintain chromosome integrity. This response may be a primitive form of sexual interaction, similar to the more well-studied bacterial transformation that is also associated with DNA transfer between cells, leading to homologous recombinational repair of DNA damage.<ref>Bernstein H, Bernstein C (2010). "Evolutionary origin of recombination during meiosis". BioScience. 60 (7): 498–505. doi:10.1525/bio.2010.60.7.5. S2CID 86663600</ref>


== Metabolism ==
== Metabolism ==
''Sulfolobus solfataricus'' is known to grow chemoorganotrophically, in presence of oxygen, on a variety of organic compounds such as sugars, alcohols, amino acids and aromatic compounds like [[phenol]].<ref name=":0">{{cite journal | vauthors = Ulas T, Riemer SA, Zaparty M, Siebers B, Schomburg D | title = Genome-scale reconstruction and analysis of the metabolic network in the hyperthermophilic archaeon Sulfolobus solfataricus | journal = PLOS ONE | volume = 7 | issue = 8 | pages = e43401 | date = 2012-08-31 | pmid = 22952675 | pmc = 3432047 | doi = 10.1371/journal.pone.0043401 | bibcode = 2012PLoSO...743401U | doi-access = free }}</ref>
''Sulfolobus solfataricus'' is known to grow by chemoorganotrophy, in the presence of oxygen, on a variety of organic compounds such as sugars, alcohols, amino acids, and aromatic compounds like [[phenol]].<ref name=":0">{{cite journal | vauthors = Ulas T, Riemer SA, Zaparty M, Siebers B, Schomburg D | title = Genome-scale reconstruction and analysis of the metabolic network in the hyperthermophilic archaeon Sulfolobus solfataricus | journal = PLOS ONE | volume = 7 | issue = 8 | pages = e43401 | date = 2012-08-31 | pmid = 22952675 | pmc = 3432047 | doi = 10.1371/journal.pone.0043401 | bibcode = 2012PLoSO...743401U | doi-access = free }}</ref>


It uses a modified [[Entner–Doudoroff pathway|Entner-Doudroff]] pathway for glucose oxidation and the resulting pyruvate molecules can be totally mineralized in [[Citric acid cycle|TCA cycle]].<ref name=":0" />
It uses a modified [[Entner–Doudoroff pathway|Entner-Doudroff]] pathway for glucose oxidation and the resulting pyruvate molecules can be totally mineralized in a [[Citric acid cycle|TCA cycle]].<ref name=":0" />


[[Oxygen|Molecular oxygen]] is the only known electron acceptor at the end of the [[electron transport chain]].<ref>{{cite journal | vauthors = Simon G, Walther J, Zabeti N, Combet-Blanc Y, Auria R, van der Oost J, Casalot L | title = Effect of O2 concentrations on Sulfolobus solfataricus P2 | journal = FEMS Microbiology Letters | volume = 299 | issue = 2 | pages = 255–60 | date = October 2009 | pmid = 19735462 | doi = 10.1111/j.1574-6968.2009.01759.x | doi-access = free }}</ref> Other than organic molecules, this [[Archaea|Archea]] species can also utilize [[hydrogen sulfide]]<ref name = "She_2001">{{cite journal | vauthors = She Q, Singh RK, Confalonieri F, Zivanovic Y, Allard G, Awayez MJ, Chan-Weiher CC, Clausen IG, Curtis BA, De Moors A, Erauso G, Fletcher C, Gordon PM, Heikamp-de Jong I, Jeffries AC, Kozera CJ, Medina N, Peng X, Thi-Ngoc HP, Redder P, Schenk ME, Theriault C, Tolstrup N, Charlebois RL, Doolittle WF, Duguet M, Gaasterland T, Garrett RA, Ragan MA, Sensen CW, Van der Oost J | display-authors = 6 | title = The complete genome of the crenarchaeon ''Sulfolobus solfataricus'' P2 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 14 | pages = 7835–40 | date = July 2001 | pmid = 11427726 | pmc = 35428 | doi = 10.1073/pnas.141222098 | bibcode = 2001PNAS...98.7835S | doi-access = free }}</ref> and [[Sulfur|elementar sulfur]] as electron donors and [[Carbon fixation|fix {{CO2}}]], possibly by means of HP/HB cycle,<ref name=":0" /> making it also capable of living chemoautotrophycally. Recent studies have found also the capability of growing, albeit slowly, oxidizing molecular hydrogen.<ref name="Sakai_2018" />
[[Oxygen|Molecular oxygen]] is the only known electron acceptor at the end of the [[electron transport chain]].<ref>{{cite journal | vauthors = Simon G, Walther J, Zabeti N, Combet-Blanc Y, Auria R, van der Oost J, Casalot L | title = Effect of O2 concentrations on Sulfolobus solfataricus P2 | journal = FEMS Microbiology Letters | volume = 299 | issue = 2 | pages = 255–60 | date = October 2009 | pmid = 19735462 | doi = 10.1111/j.1574-6968.2009.01759.x | doi-access = free }}</ref> Other than organic molecules, this [[Archaea]] species can also utilize [[hydrogen sulfide]]<ref name = "She_2001">{{cite journal | vauthors = She Q, Singh RK, Confalonieri F, Zivanovic Y, Allard G, Awayez MJ, Chan-Weiher CC, Clausen IG, Curtis BA, De Moors A, Erauso G, Fletcher C, Gordon PM, Heikamp-de Jong I, Jeffries AC, Kozera CJ, Medina N, Peng X, Thi-Ngoc HP, Redder P, Schenk ME, Theriault C, Tolstrup N, Charlebois RL, Doolittle WF, Duguet M, Gaasterland T, Garrett RA, Ragan MA, Sensen CW, Van der Oost J | display-authors = 6 | title = The complete genome of the crenarchaeon ''Sulfolobus solfataricus'' P2 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 14 | pages = 7835–40 | date = July 2001 | pmid = 11427726 | pmc = 35428 | doi = 10.1073/pnas.141222098 | bibcode = 2001PNAS...98.7835S | doi-access = free }}</ref> and [[Sulfur|elementary sulfur]] as electron donors and [[Carbon fixation|fix {{CO2}}]], possibly by means of the HP/HB cycle,<ref name=":0" /> making it also capable of living by chemoautotrophy. <!-- Consider describing the HP/HB cycle. -->Recent studies have also found the capability of growing, albeit slowly, by oxidizing molecular hydrogen.<ref name="Sakai_2018" />


===''Ferredoxin''===
===''Ferredoxin''===
[[Ferredoxin]] is suspected to act as the major metabolic electron carrier in ''S. solfataricus''. This contrasts with most species within the Bacteria and Eukarya, which generally rely on [[NADH]] as the main electron carrier. ''S. solfataricus'' has strong eukaryotic features coupled with many uniquely archaeal-specific abilities. The results of the findings came from the varied methods of their DNA mechanisms, cell cycles, and transitional apparatus. Overall, the study was a prime example of the differences found in [[Thermoproteota]] and "[[Euryarchaeota]]".<ref name="She_2001" /><ref>{{cite journal|vauthors=Zillig W, Stetter KO, Wunderl S, Schulz W, Priess H, Scholz I|date=April 1980|title=The Sulfolobus-"Caldariella" group: taxonomy on the basis of the structure of DNA-dependent RNA polymerases.|journal=Archives of Microbiology|volume=125|issue=3|pages=259–69|doi=10.1007/BF00446886|s2cid=5805400}}</ref>
[[Ferredoxin]] is suspected to act as the major metabolic electron carrier in ''S. solfataricus''. This contrasts with most species within the Bacteria and Eukaryote groups of organisms, which generally rely on nicotinamide adenine dinucleotide hydrogen ([[NADH]]) as the main electron carrier. ''S. solfataricus'' has strong eukaryotic features coupled with many uniquely archaeal-specific abilities. The results of the findings came from the varied methods of their DNA mechanisms, cell cycles, and transitional apparatus. Overall, the study was a prime example of the differences found in [[Thermoproteota]] and "[[Euryarchaeota]]".<ref name="She_2001" /><ref>{{cite journal|vauthors=Zillig W, Stetter KO, Wunderl S, Schulz W, Priess H, Scholz I|date=April 1980|title=The Sulfolobus-"Caldariella" group: taxonomy on the basis of the structure of DNA-dependent RNA polymerases.|journal=Archives of Microbiology|volume=125|issue=3|pages=259–69|doi=10.1007/BF00446886|s2cid=5805400}}</ref>


== Ecology ==
== Ecology ==


===''Habitat''===
===''Habitat''===
⚫
[[File:Solfatara_volcano.jpg|right|thumb|300x300px|Fumarole of Solfatara volcano - Campania, Italy.]]
''S. solfataricus'' is an extreme thermophile Archea, as the rest of the species of the genus Sulfolobus, it has optimal growth conditions in strong volcanic activity areas, with high temperature and very acid pH,<ref>{{cite journal | vauthors = Grogan DW | title = Phenotypic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains | journal = Journal of Bacteriology | volume = 171 | issue = 12 | pages = 6710–9 | date = December 1989 | pmid = 2512283 | pmc = 210567 | doi = 10.1128/jb.171.12.6710-6719.1989 }}</ref> these specific conditions are typical of volcanic area as geyser or thermal springs, in fact the most studied countries where microorganism were found are: U.S.A (Yellowstone National Park),<ref>{{cite web|url=https://microbewiki.kenyon.edu/index.php/Sulfolobus|title=Sulfolobus|website=Microbewiki}}</ref> New Zealand,<ref>{{cite journal | vauthors = Hetzer A, Morgan HW, McDonald IR, Daughney CJ | title = Microbial life in Champagne Pool, a geothermal spring in Waiotapu, New Zealand | journal = Extremophiles | volume = 11 | issue = 4 | pages = 605–14 | date = July 2007 | pmid = 17426919 | doi = 10.1007/s00792-007-0073-2 | s2cid = 24239907 }}</ref> Island and Italy, notoriously famous for volcanic phenomena like these. A study conducted by a team of Indonesian scientists has shown the presence of a Sulfolobus community also in the West Java, confirming that high fears, low ph and sulfur presence are necessary conditions for the growth of these microbes.<ref>{{cite journal | vauthors = Aditiawati P, Yohandini H, Madayanti F | title = Microbial diversity of acidic hot spring (kawah hujan B) in geothermal field of kamojang area, west java-indonesia | journal = The Open Microbiology Journal | volume = 3 | pages = 58–66 | year = 2009 | pmid = 19440252 | pmc = 2681175 | doi = 10.2174/1874285800903010058 }}</ref>
''S. solfataricus'' is an extreme thermophile Archaea, as the rest of the species of the genus ''Sulfolobus'', has optimal growth conditions in strong volcanic activity areas, with high temperatures and very acidic pH<ref>{{cite journal | vauthors = Grogan DW | title = Phenotypic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains | journal = Journal of Bacteriology | volume = 171 | issue = 12 | pages = 6710–9 | date = December 1989 | pmid = 2512283 | pmc = 210567 | doi = 10.1128/jb.171.12.6710-6719.1989 }}</ref>. These specific conditions are typical of volcanic areas such as geyser or thermal springs. In fact, the most studied countries where these microorganisms were found are U.S.A. (Yellowstone National Park),<ref>{{cite web|url=https://microbewiki.kenyon.edu/index.php/Sulfolobus|title=Sulfolobus|website=Microbewiki}}</ref> New Zealand,<ref>{{cite journal | vauthors = Hetzer A, Morgan HW, McDonald IR, Daughney CJ | title = Microbial life in Champagne Pool, a geothermal spring in Waiotapu, New Zealand | journal = Extremophiles | volume = 11 | issue = 4 | pages = 605–14 | date = July 2007 | pmid = 17426919 | doi = 10.1007/s00792-007-0073-2 | s2cid = 24239907 }}</ref> Island and Italy, notoriously famous for volcanic phenomena. <!-- Which Island? I think the name of the Island is missing. -->A study conducted by a team of Indonesian scientists has also shown the presence of a ''Sulfolobus'' community in West Java, confirming that high temperatures, low pH, and the presence of sulfur are necessary conditions for the growth of these microbes.<ref>{{cite journal | vauthors = Aditiawati P, Yohandini H, Madayanti F | title = Microbial diversity of acidic hot spring (kawah hujan B) in geothermal field of kamojang area, west java-indonesia | journal = The Open Microbiology Journal | volume = 3 | pages = 58–66 | year = 2009 | pmid = 19440252 | pmc = 2681175 | doi = 10.2174/1874285800903010058 |doi-access=free}}</ref>
⚫
[[File:Solfatara_volcano.jpg|left|thumb|300x300px|Fumarole of Solfatara volcano - Campania, Italy.]]


===''Soil acidification''===
===''Soil acidification''===
''S. solfataricus'' is able to oxidize sulfur according to metabolic strategy, one of the products of these reactions is H+ and, consequentially, it results in a slowly acidification of surrounding area. Soil acidification increase in place where there are emissions of pollutants from industrial activity, and this process reduce the number of heterotrophic bacterial involved to decomposition, which are fundamental to recycling organic matter and ultimately to fertilizing soil.<ref>{{cite journal | vauthors = Bryant RD, Gordy EA, Laishley EJ |title=Effect of soil acidification on the soil microflora|journal=Water, Air, and Soil Pollution |volume=11 |issue=4 |pages=437 |doi=10.1007/BF00283435 |year=1979 |bibcode=1979WASP...11..437B |s2cid=96729369}}</ref>
''S. solfataricus'' is able to oxidize sulfur according to metabolic strategy. One of the products of these reactions is H+ and, consequentially, it results in a slowly acidification of the surrounding area. Soil acidification increases in places where there are emissions of pollutants from industrial activity, and this process reduces the number of heterotrophic bacteria involved in decomposition, which are fundamental to recycling organic matter and ultimately to fertilizing soil.<ref>{{cite journal | vauthors = Bryant RD, Gordy EA, Laishley EJ |title=Effect of soil acidification on the soil microflora|journal=Water, Air, and Soil Pollution |volume=11 |issue=4 |pages=437 |doi=10.1007/BF00283435 |year=1979 |bibcode=1979WASP...11..437B |s2cid=96729369}}</ref>
{{clear}}
{{clear}}


== Biotechnologie: Untapping the resource ''Sulfolobus''==
== Biotechnology: Untapping the resource ''Sulfolobus''==
Today, in many fields of application, we are interested in using ''Sulfolobus sulfataricus'' as a source of thermal stability enzymes for research and diagnostics, as well as in the food, textile and cleaning industries, and the pulp and paper industry. Furthermore, this enzyme is overloaded due to its catalytic diversity, high pH and temperature stability, increased to organic solvents and resistance to proteolysis.<ref>{{Cite journal|last=Stepankova|first=Veronika|date=October 14, 2013|title=Strategies for Stabilization of Enzymes in Organic Solvents|journal=ACS Catalysis|volume=3|issue=12|pages=2823–2836|doi=10.1021/cs400684x}}</ref><ref>{{Cite journal|last=DANIEL|first=R. M.|date=1982|title=A correlation between protein thermostability and resistance to proteolysis|journal= Biochemical Journal|volume=207|issue=3|pages=641–644|pmc=1153914|pmid=6819862|doi=10.1042/bj2070641}}</ref>
Today, in many fields of application, there is interest in using ''S. sulfataricus'' as a source of thermal stability enzymes for research and diagnostics as well as in the food, textile, cleaning, and pulp and paper industries. Furthermore, this enzyme is overloaded due to its catalytic diversity, high pH, and temperature stability, increased to organic solvents and resistance to proteolysis.<ref>{{Cite journal|last=Stepankova|first=Veronika|date=October 14, 2013|title=Strategies for Stabilization of Enzymes in Organic Solvents|journal=ACS Catalysis|volume=3|issue=12|pages=2823–2836|doi=10.1021/cs400684x}}</ref><ref>{{Cite journal|last=DANIEL|first=R. M.|date=1982|title=A correlation between protein thermostability and resistance to proteolysis|journal= Biochemical Journal|volume=207|issue=3|pages=641–644|pmc=1153914|pmid=6819862|doi=10.1042/bj2070641}}</ref> <!-- Why is it overloaded? What does "increased to organic solvents" mean? -->


At present, tetraester lipids, membrane vesicles with antimicrobial properties, trehalose components, and new β-galactooligosaccharides are coming increasingly important.<ref name=":02">{{Cite journal|last=Quehenberger|first=Julian|date=2017|title=Sulfolobus – A Potential Key Organism in Future Biotechnology|journal= Frontiers in Microbiology|volume=8|pages=2474|doi=10.3389/fmicb.2017.02474|pmid=29312184|pmc=5733018|doi-access=free}}</ref>
At present, tetra ester lipids, membrane vesicles with antimicrobial properties, trehalose components, and new β-galactooligosaccharides are becoming increasingly important.<ref name=":02">{{Cite journal|last=Quehenberger|first=Julian|date=2017|title=Sulfolobus – A Potential Key Organism in Future Biotechnology|journal= Frontiers in Microbiology|volume=8|pages=2474|doi=10.3389/fmicb.2017.02474|pmid=29312184|pmc=5733018|doi-access=free}}</ref>


=== β-galactosidase ===
=== β-galactosidase ===


{{see also|Beta-galactosidase}}
{{see also|Beta-galactosidase}}
The thermostable enzyme [[Beta-galactosidase|β-galactosidase]] isolated from the extreme thermophile archaebacterial ''Sulfolobus solfataricus, strain MT-4.''
The thermostable enzyme [[Beta-galactosidase|β-galactosidase]] was isolated from the extreme thermophile archaebacterial ''S. solfataricus, strain MT-4.''


This enzyme utilized on many industrial process of lactose containing fluids by purifying and characterizing for their physicochemical properties.<ref>{{Cite journal|last=M. PISANI|first=Francesca|date=1990|title=Thermostable P-galactosidase from the archaebacterium Sulfolobus solfataricus|journal= European Journal of Biochemistry|volume=187|issue=2|pages=321–328|doi=10.1111/j.1432-1033.1990.tb15308.x|pmid=2105216}}</ref>
This enzyme is utilized in many industrial processes of lactose containing fluids by purifying and characterizing their physicochemical properties.<ref>{{Cite journal|last=M. PISANI|first=Francesca|date=1990|title=Thermostable P-galactosidase from the archaebacterium Sulfolobus solfataricus|journal= European Journal of Biochemistry|volume=187|issue=2|pages=321–328|doi=10.1111/j.1432-1033.1990.tb15308.x|pmid=2105216|doi-access=free}}</ref> <!-- Consider adding a few example of these industrial processes. -->


=== Proteases ===
=== Proteases ===


{{see also|Protease}}
{{see also|Protease}}
The industry are interested in stable proteases as well as in many different sulfolobus proteases that have been studied.<ref>{{Cite book|title=Isolation and characterization of an intracellular aminopeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus|journal = Biochimica et Biophysica Acta (BBA) - General Subjects|volume = 1033|issue = 2|last=Hanner|first=Markus|publisher=Elsevier B.V.|year=1990|isbn=0117536121|pages=148–153|doi = 10.1016/0304-4165(90)90005-H|pmid = 2106344}}</ref>
The industry are interested in stable proteases as well as in many different ''Sulfolobus'' proteases that have been studied.<ref>{{Cite book|title=Isolation and characterization of an intracellular aminopeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus|journal = Biochimica et Biophysica Acta (BBA) - General Subjects|volume = 1033|issue = 2|last=Hanner|first=Markus|publisher=Elsevier B.V.|year=1990|isbn=0117536121|pages=148–153|doi = 10.1016/0304-4165(90)90005-H|pmid = 2106344}}</ref> <!-- Which industry is interested? -->


An active [[aminopeptidase]] associated with the [[Chaperonin ATPase|chaperonin]] of Solfobulus solfataricus MT4 was described''.''<ref>{{Cite journal|last1=Condo|first1=Ivano|last2=Ruggero|first2=Davide|date=1998|title=A novel aminopeptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus. Mol. Microbiol.|journal= Molecular Microbiology|volume=29|issue=3|pages=775–785|doi=10.1046/j.1365-2958.1998.00971.x|pmid=9723917|doi-access=free}}</ref>
An active [[aminopeptidase]] associated with the [[Chaperonin ATPase|chaperonin]] of ''S. solfataricus'' MT4 was described''.''<ref>{{Cite journal|last1=Condo|first1=Ivano|last2=Ruggero|first2=Davide|date=1998|title=A novel aminopeptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus. Mol. Microbiol.|journal= Molecular Microbiology|volume=29|issue=3|pages=775–785|doi=10.1046/j.1365-2958.1998.00971.x|pmid=9723917|doi-access=free}}</ref>


Sommaruga et al.(2014)<ref name=":1">{{Cite journal|last=Sommaruga|first=Silvia|date=2014|title=mmobilization of carboxypeptidase from Sulfolobus solfataricus on magnetic nanoparticles improves enzyme stability and functionality in organic media. BMC Biotechnol.|journal= BMC Biotechnology|volume=14|issue=1|pages=82|doi=10.1186/1472-6750-14-82|pmid=25193105|pmc=4177664}}</ref> also improved the stability and reaction yield of a well-characterized [[carboxypeptidase]] from S.solfataricus MT4 by magnetic nanoparticles immobilizing the enzyme.
Sommaruga et al. (2014)<ref name=":1">{{Cite journal|last=Sommaruga|first=Silvia|date=2014|title=mmobilization of carboxypeptidase from Sulfolobus solfataricus on magnetic nanoparticles improves enzyme stability and functionality in organic media. BMC Biotechnol.|journal= BMC Biotechnology|volume=14|issue=1|pages=82|doi=10.1186/1472-6750-14-82|pmid=25193105|pmc=4177664 |doi-access=free }}</ref> also improved the stability and reaction yield of a well-characterized [[carboxypeptidase]] from ''S. solfataricus'' MT4 by magnetic nanoparticles immobilizing the enzyme.


=== [[Esterase]]s/Lipases ===
=== [[Esterase]]s/Lipases ===


{{see also|Lipase}}
{{see also|Lipase}}
A new thermostable extracellular lipolytic enzyme [[Serine protease|serine]] [[arylesterase]] which is originally discovered for their large action in the hydrolysis of [[organophosphate]]s from the thermoacidophilic archaeon ''Sulfolobus solfataricus P1''.<ref>{{Cite journal|last=Park|first=Young-Jun|date=2016|title= Purification and characterization of a new inducible thermostable extracellular lipolytic enzyme from the thermoacidophilic archaeon Sulfolobus solfataricus P1|journal= Journal of Molecular Catalysis B: Enzymatic|volume=124|pages=11–19|doi=10.1016/j.molcatb.2015.11.023}}</ref>
A new thermostable extracellular lipolytic enzyme [[Serine protease|serine]] [[arylesterase]] was originally discovered for their large action in the hydrolysis of [[organophosphate]]s from the thermoacidophilic archaeon ''S. solfataricus P1''.<ref>{{Cite journal|last=Park|first=Young-Jun|date=2016|title= Purification and characterization of a new inducible thermostable extracellular lipolytic enzyme from the thermoacidophilic archaeon Sulfolobus solfataricus P1|journal= Journal of Molecular Catalysis B: Enzymatic|volume=124|pages=11–19|doi=10.1016/j.molcatb.2015.11.023}}</ref> <!-- What is the large action? -->


=== Chaperonins ===
=== Chaperonins ===


{{see also|Chaperonin ATPase}}
{{see also|Chaperonin ATPase}}
In reaction to temperature shock (50.4&nbsp;°C) in [[Escherichia coli|E.Coli]] cells, a tiny warm stun protein (S.so-HSP20) from S.solfataricus P2 has been effectively used to improve tolerance.<ref>{{Cite journal|last=Li|first=Dong-Chol|date=August 2011|title=Thermotolerance and molecular chaperone function of the small heat shock protein HSP20 from hyperthermophilic archaeon, Sulfolobus solfataricus P2. Cell Stress Chaperones|journal= Cell Stress & Chaperones|volume=17|issue=1|pages=103–108|doi=10.1007/s12192-011-0289-z|pmid=21853411|pmc=3227843}}</ref>
In reaction to temperature shock (50.4 °C) in [[Escherichia coli|E. coli]] cells, a tiny warm stun protein (S.so-HSP20) from ''S.solfataricus'' P2 has been effectively used to improve tolerance to temperature.<ref>{{Cite journal|last=Li|first=Dong-Chol|date=August 2011|title=Thermotolerance and molecular chaperone function of the small heat shock protein HSP20 from hyperthermophilic archaeon, Sulfolobus solfataricus P2. Cell Stress Chaperones|journal= Cell Stress & Chaperones|volume=17|issue=1|pages=103–108|doi=10.1007/s12192-011-0289-z|pmid=21853411|pmc=3227843}}</ref>


In view of the fact that chaperonin Ssocpn (920 kDa), which includes [[Adenosine triphosphate|ATP]], K+ and Mg2 + but has not produced any additional proteins in S.solfataricus to supply collapsed and dynamic proteins from denatured materials, it was stored on an ultrafiltration cell, while the renatured substrates were moving through the film.<ref>{{Cite journal|last=Cerchia|first=Laura|date=7 August 1999|title=An archaeal chaperonin-based reactor for renaturation of denatured proteins. Extremophile|journal= Extremophiles: Life Under Extreme Conditions|volume=4|issue=1|pages=1–7|doi=10.1007/s007920050001|pmid=10741831|s2cid=25407893}}</ref>
In view of the fact that chaperonin Ssocpn (920 kDa), which includes adenosine triphosphate ([[Adenosine triphosphate|ATP]]), K+, and Mg<sup>2</sup> +, has not produced any additional proteins in ''S. solfataricus'' to supply collapsed and dynamic proteins from denatured materials, it was stored on an ultrafiltration cell, while the renatured substrates were moving through the film.<ref>{{Cite journal|last=Cerchia|first=Laura|date=7 August 1999|title=An archaeal chaperonin-based reactor for renaturation of denatured proteins. Extremophile|journal= Extremophiles: Life Under Extreme Conditions|volume=4|issue=1|pages=1–7|doi=10.1007/s007920050001|pmid=10741831|s2cid=25407893}}</ref>


=== Liposomes ===
=== Liposomes ===

{{see also|Liposome}}
{{see also|Liposome}}
Because of its tetraether lipid material, the membrane of extreme thermophilic Archaea is unique in its composition. Archaea lipids are a promising source of liposomes with exceptional stability of temperature and pH and tightness against leakage of solute. Such archaeosomes are possible instruments for the delivery of medicines, vaccines, and genes.<ref>{{Cite journal|last=B. Patel|first=Girishchandra|date=1999|title=Archaeobacterial Ether Lipid Liposomes (Archaeosomes) as Novel Vaccine and Drug Delivery Systems|journal=Critical Reviews in Biotechnology|volume=19|issue=4|pages=317–357|doi=10.1080/0738-859991229170|pmid=10723627}}</ref>
Because of its tetraether lipid material, the membrane of extreme thermophilic Archaea is unique in its composition. Archaea lipids are a promising source of liposomes with exceptional stability of temperature, pH, and tightness against the leakage of solute. Such archaeosomes are possible instruments for the delivery of medicines, vaccines, and genes.<ref>{{Cite journal|last=B. Patel|first=Girishchandra|date=1999|title=Archaeobacterial Ether Lipid Liposomes (Archaeosomes) as Novel Vaccine and Drug Delivery Systems|journal=Critical Reviews in Biotechnology|volume=19|issue=4|pages=317–357|doi=10.1080/0738-859991229170|pmid=10723627}}</ref>

==See also==
* [[List of Archaea genera]]


== References ==
== References ==
Line 110: Line 115:
* {{cite journal | vauthors = Fiorentino G, Del Giudice I, Petraccone L, Bartolucci S, Del Vecchio P | title = Conformational stability and ligand binding properties of BldR, a member of the MarR family, from Sulfolobus solfataricus | journal = Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | volume = 1844 | issue = 6 | pages = 1167–72 | date = June 2014 | pmid = 24704039 | doi = 10.1016/j.bbapap.2014.03.011 }}<!--|access-date=11 November 2014-->
* {{cite journal | vauthors = Fiorentino G, Del Giudice I, Petraccone L, Bartolucci S, Del Vecchio P | title = Conformational stability and ligand binding properties of BldR, a member of the MarR family, from Sulfolobus solfataricus | journal = Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | volume = 1844 | issue = 6 | pages = 1167–72 | date = June 2014 | pmid = 24704039 | doi = 10.1016/j.bbapap.2014.03.011 }}<!--|access-date=11 November 2014-->
* {{cite journal | vauthors = de Rosa M, Bemporad F, Pellegrino S, Chiti F, Bolognesi M, Ricagno S | title = Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase | journal = The FEBS Journal | volume = 281 | issue = 18 | pages = 4072–84 | date = September 2014 | pmid = 24893801 | doi = 10.1111/febs.12861 | doi-access = free }}
* {{cite journal | vauthors = de Rosa M, Bemporad F, Pellegrino S, Chiti F, Bolognesi M, Ricagno S | title = Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase | journal = The FEBS Journal | volume = 281 | issue = 18 | pages = 4072–84 | date = September 2014 | pmid = 24893801 | doi = 10.1111/febs.12861 | doi-access = free }}
* {{cite journal | vauthors = Gamsjaeger R, Kariawasam R, Touma C, Kwan AH, White MF, Cubeddu L | title = Backbone and side-chain ¹H, ¹³C and ¹⁵N resonance assignments of the OB domain of the single stranded DNA binding protein from Sulfolobus solfataricus and chemical shift mapping of the DNA-binding interface | journal = Biomolecular NMR Assignments | volume = 8 | issue = 2 | pages = 243–6 | date = October 2014 | pmid = 23749431 | doi = 10.1007/s12104-013-9492-4 | s2cid = 6388231 }}
* {{cite journal | vauthors = Gamsjaeger R, Kariawasam R, Touma C, Kwan AH, White MF, Cubeddu L | title = Backbone and side-chain <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N resonance assignments of the OB domain of the single stranded DNA binding protein from Sulfolobus solfataricus and chemical shift mapping of the DNA-binding interface | journal = Biomolecular NMR Assignments | volume = 8 | issue = 2 | pages = 243–6 | date = October 2014 | pmid = 23749431 | doi = 10.1007/s12104-013-9492-4 | s2cid = 6388231 }}
* {{cite journal | vauthors = Wang J, Zhu J, Min C, Wu S | title = CBD binding domain fused γ-lactamase from Sulfolobus solfataricus is an efficient catalyst for (-) γ-lactam production | journal = BMC Biotechnology | volume = 14 | pages = 40 | date = May 2014 | pmid = 24884655 | pmc = 4041915 | doi = 10.1186/1472-6750-14-40 }}
* {{cite journal | vauthors = Wang J, Zhu J, Min C, Wu S | title = CBD binding domain fused γ-lactamase from Sulfolobus solfataricus is an efficient catalyst for (-) γ-lactam production | journal = BMC Biotechnology | volume = 14 | pages = 40 | date = May 2014 | pmid = 24884655 | pmc = 4041915 | doi = 10.1186/1472-6750-14-40 | doi-access = free }}
{{refend}}
{{refend}}
'


== External links ==
== External links ==
*[http://bacdive.dsmz.de/index.php?search=16650&submit=Search Type strain of ''Sulfolobus solfataricus'' at Bac''Dive'' - the Bacterial Diversity Metadatabase]
*[http://bacdive.dsmz.de/index.php?search=16650&submit=Search Type strain of ''Sulfolobus solfataricus'' at Bac''Dive'' - the Bacterial Diversity Metadatabase]


{{Archaea classification}}
{{Taxonbar|from=Q3503466}}
{{Taxonbar|from=Q3503466}}


Revision as of 19:09, 18 December 2024

Sulfolobus solfataricus
Scientific classification
Domain:
Archaea
Phylum:
Thermoproteota
Class:
Thermoprotei
Order:
Sulfolobales
Family:
Sulfolobaceae
Genus:
Sulfolobus
Species:
S. solfataricus
Binomial name
Sulfolobus solfataricus
Zillig et al. 1980
Synonyms
  • Saccharolobus solfataricus (Zillig et al. 1980) Sakai & Kurosawa 2018

Saccharolobus solfataricus is a species of thermophilic archaeon. It was transferred from the genus Sulfolobus to the new genus Saccharolobus with the description of Saccharolobus caldissimus in 2018.[1]

It was first discovered and isolated from the Solfatara volcano (Pisciarelli-Campania, Italy) in 1980 by two German microbiologists Karl Setter and Wolfram Zillig.[2]

However, these organisms are not isolated to volcanoes but are found all over the world in places such as hot springs. The species grows best in temperatures around 80 °C, a pH level between 2 and 4, and with enough sulfur for S. solfataricus to metabolize in order to gain energy. These conditions qualify it as an extremophile and it is specifically known as a thermoacidophile because of its preference for high temperatures and low pH levels. It is also aerobic and heterotropic due to its metabolic system.[3] Being an autotroph, it receives energy by growing on sulfur or even a variety of organic compounds.[4] It usually has a spherical cell shape and it makes frequent lobes.

Currently, it is the most widely studied organism within the Thermoproteota branch. Solfataricus are examined for their methods of DNA replication, cell cycle, chromosomal integration, transcription, RNA processing, and translation. All of the data points to the organism having a large percent of archaeal-specific genes, which shows the differences between the three types of microbes: archaea, bacteria, and eukaryote.

Genome

Sulfolobus solfataricus is the most studied microorganism from a molecular, genetic, and biochemical point of view for its ability to thrive in extreme environments. It can grow easily in the laboratory; moreover, it can exchange genetic material through processes of transformation, transduction. and conjugation.

The major motivation for sequencing these microorganisms is the thermostability of proteins that normally denature at a high temperature. The complete sequence the genome of S. solfataricus was completed in 2001.[5] On a single chromosome, there are 2,992,245 base pairs which encode for 2,977 proteins and copious RNAs. One-third of S. solfataricus encoded proteins have no homologs in other genomes. For the remaining encoded proteins, 40% are specific to Archaea, 12% are shared with Bacteria, and 2.3% are shared with Eukaryote;[6] 33% of these proteins are encoded exclusively in Sulfolobus. A high number of open reading frames (ORFs) are highly similar in Thermoplasma.[3]

Small nucleolar RNAs (snoRNAs), already present in eukaryotes, have also been identified in S. solfataricus and S. acidolcaldarius. They are already known for the role they play in post-transcriptional modifications and removal of introns from ribosomal RNA in Eukaryote.[7]

The genome of Sulfolobus is characterized by the presence of short tandem repeats, insertion and repetitive elements. It has a wide range of diversity with 200 different insertion sequence elements.

Thermophilic reverse gyrase

The stabilization of the double helix against denaturation, in the Archaea, is due to the presence of a particular thermophilic enzyme, reverse gyrase. It was discovered in hyper-thermophilic and thermophilic Archaea and Bacteria. There are two genes in Sulfolobus that each encode a reverse gyrase.[8] It is defined as an atypical DNA topoisomerase and the basic activity consists of the production of positive supercoils in a closed circular DNA. Positive supercoiling is important to prevent the formation of open complexes. Reverse gyrases are composed of two domains: the first one is the helicase and second one is the topoisomerase I. A possible role of reverse gyrase could be the use of positive supercoiling to assemble chromatin-like structures.[9] In 1997, scientists discovered another important feature of Sulfolobus: a type-II topoisomerase, called TopoVI, whose A subunit is homologous to the meiotic recombination factor, Spo11, which plays a predominant role in the initiation of meiotic recombination in all Eukaryotes.[10][11]

S. solfataricus is composed of three topoisomerases of type I, TopA and two reverse gyrases, TopR1 and TopR2, and one topoisomerase of type II, TopoVI.[12]

DNA binding proteins

In the phylum Thermoproteota, there are three proteins that bind to the minor groove of DNA-like histones, Alba, Cren7, and Sso7d, that are modified after the translation process. These histones are small and have been found in several strains of Sulfolobus but not in other genomes. Chromatin protein in Sulfolobus represent 1-5% of the total genome. They can have both structural and regulatory functions. These look like human HMG-box proteins, because of their influence on genomes, expression and stability, and epigenetic processes.[13] In species lacking histones, they can be acetylated and methylated like eukaryotic histones.[14][15][16][17] Sulfolobus strains present different peculiar DNA binding proteins, such as the Sso7d protein family. They stabilize the double helix, preventing denaturation at high temperature and thus promoting annealing above the melting point.[18]

The major component of Archaea chromatin is represented by Sac10b family protein known as Alba (acetylation lowers binding affinity).[19][20] These proteins are small, basic, and dimeric nucleic acid-binding proteins. Furthermore, it is conserved in most sequenced Archaea genomes.[21][22] The acetylation state of Alba affects promoter access and transcription in vitro, whereas the methylation state of another Sulfolobus chromatin protein, Sso7D, is altered by culture temperature.[23][24]

The work of Wolfram Zillig's group, representing early evidence of the eukaryotic characteristics of transcription in Archaea, has since made Sulfolobus an ideal model system for transcription studies. Recent studies in Sulfolobus, in addition to other Archaea species, mainly focus on the composition, function, and regulation of the transcription machinery and on fundamental conserved aspects of this process in both Eukaryotes and Archaea.[25]

DNA transfer

Exposure of Saccharolobus solfataricus to the DNA damaging agents, ultraviolet (UV) irradiation, bleomycin, or mitomycin C, induces cellular aggregation.[26] Other physical stressors, such as changes in pH or temperature shift, do not induce aggregation, suggesting that the induction of aggregation is caused specifically by DNA damage. Ajon et al.[27] showed that UV-induced cellular aggregation mediates chromosomal marker exchange with high frequency. Recombination rates exceeded those of uninduced cultures by up to three orders of magnitude. Frols et al.[26][28] and Ajon et al.[27] hypothesized that the UV-induced DNA transfer process and subsequent homologous recombinational repair represents an important mechanism to maintain chromosome integrity. This response may be a primitive form of sexual interaction, similar to the more well-studied bacterial transformation that is also associated with DNA transfer between cells, leading to homologous recombinational repair of DNA damage.[29]

Metabolism

Sulfolobus solfataricus is known to grow by chemoorganotrophy, in the presence of oxygen, on a variety of organic compounds such as sugars, alcohols, amino acids, and aromatic compounds like phenol.[30]

It uses a modified Entner-Doudroff pathway for glucose oxidation and the resulting pyruvate molecules can be totally mineralized in a TCA cycle.[30]

Molecular oxygen is the only known electron acceptor at the end of the electron transport chain.[31] Other than organic molecules, this Archaea species can also utilize hydrogen sulfide[6] and elementary sulfur as electron donors and fix CO2, possibly by means of the HP/HB cycle,[30] making it also capable of living by chemoautotrophy. Recent studies have also found the capability of growing, albeit slowly, by oxidizing molecular hydrogen.[1]

Ferredoxin

Ferredoxin is suspected to act as the major metabolic electron carrier in S. solfataricus. This contrasts with most species within the Bacteria and Eukaryote groups of organisms, which generally rely on nicotinamide adenine dinucleotide hydrogen (NADH) as the main electron carrier. S. solfataricus has strong eukaryotic features coupled with many uniquely archaeal-specific abilities. The results of the findings came from the varied methods of their DNA mechanisms, cell cycles, and transitional apparatus. Overall, the study was a prime example of the differences found in Thermoproteota and "Euryarchaeota".[6][32]

Ecology

Habitat

Fumarole of Solfatara volcano - Campania, Italy.

S. solfataricus is an extreme thermophile Archaea, as the rest of the species of the genus Sulfolobus, has optimal growth conditions in strong volcanic activity areas, with high temperatures and very acidic pH[33]. These specific conditions are typical of volcanic areas such as geyser or thermal springs. In fact, the most studied countries where these microorganisms were found are U.S.A. (Yellowstone National Park),[34] New Zealand,[35] Island and Italy, notoriously famous for volcanic phenomena. A study conducted by a team of Indonesian scientists has also shown the presence of a Sulfolobus community in West Java, confirming that high temperatures, low pH, and the presence of sulfur are necessary conditions for the growth of these microbes.[36]

Soil acidification

S. solfataricus is able to oxidize sulfur according to metabolic strategy. One of the products of these reactions is H+ and, consequentially, it results in a slowly acidification of the surrounding area. Soil acidification increases in places where there are emissions of pollutants from industrial activity, and this process reduces the number of heterotrophic bacteria involved in decomposition, which are fundamental to recycling organic matter and ultimately to fertilizing soil.[37]

Biotechnology: Untapping the resource Sulfolobus

Today, in many fields of application, there is interest in using S. sulfataricus as a source of thermal stability enzymes for research and diagnostics as well as in the food, textile, cleaning, and pulp and paper industries. Furthermore, this enzyme is overloaded due to its catalytic diversity, high pH, and temperature stability, increased to organic solvents and resistance to proteolysis.[38][39]

At present, tetra ester lipids, membrane vesicles with antimicrobial properties, trehalose components, and new β-galactooligosaccharides are becoming increasingly important.[40]

β-galactosidase

See also: Beta-galactosidase

The thermostable enzyme β-galactosidase was isolated from the extreme thermophile archaebacterial S. solfataricus, strain MT-4.

This enzyme is utilized in many industrial processes of lactose containing fluids by purifying and characterizing their physicochemical properties.[41]

Proteases

See also: Protease

The industry are interested in stable proteases as well as in many different Sulfolobus proteases that have been studied.[42]

An active aminopeptidase associated with the chaperonin of S. solfataricus MT4 was described.[43]

Sommaruga et al. (2014)[44] also improved the stability and reaction yield of a well-characterized carboxypeptidase from S. solfataricus MT4 by magnetic nanoparticles immobilizing the enzyme.

Esterases/Lipases

See also: Lipase

A new thermostable extracellular lipolytic enzyme serine arylesterase was originally discovered for their large action in the hydrolysis of organophosphates from the thermoacidophilic archaeon S. solfataricus P1.[45]

Chaperonins

See also: Chaperonin ATPase

In reaction to temperature shock (50.4 °C) in E. coli cells, a tiny warm stun protein (S.so-HSP20) from S.solfataricus P2 has been effectively used to improve tolerance to temperature.[46]

In view of the fact that chaperonin Ssocpn (920 kDa), which includes adenosine triphosphate (ATP), K+, and Mg2 +, has not produced any additional proteins in S. solfataricus to supply collapsed and dynamic proteins from denatured materials, it was stored on an ultrafiltration cell, while the renatured substrates were moving through the film.[47]

Liposomes

See also: Liposome

Because of its tetraether lipid material, the membrane of extreme thermophilic Archaea is unique in its composition. Archaea lipids are a promising source of liposomes with exceptional stability of temperature, pH, and tightness against the leakage of solute. Such archaeosomes are possible instruments for the delivery of medicines, vaccines, and genes.[48]

See also

References

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Further reading

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