CAMP receptor protein: Difference between revisions
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{{Short description|Regulatory protein in bacteria}} |
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{{mergeto|Catabolite_activator_protein|Talk:Catabolite_activator_protein#Merger proposal|date=December 2007}} |
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{{Lowercase}} |
{{Lowercase}} |
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{{Distinguish|C-reactive protein}} |
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{{Protein |
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{{Infobox protein |
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|Name={{PAGENAME}} |
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|Name=CAMP receptor protein |
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|image= |
|image=1i5z.jpg |
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|caption=Structure of the ''E. coli'' Cyclic AMP Receptor Protein. |
|caption=Structure of the ''E. coli'' Cyclic AMP Receptor Protein. |
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|Symbol=CRP |
|Symbol=CRP |
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|AltSymbols=CAP |
|AltSymbols=CAP |
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|EntrezGene= |
|EntrezGene=947867 |
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|RefSeq= |
|RefSeq=NP_417816.1 |
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|UniProt= |
|UniProt=P0ACJ8 |
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|PDB=1I5Z |
|PDB=1I5Z |
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}} |
}} |
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'''cAMP receptor protein''' ('''CRP'''; also known as '''[[catabolite activator protein]]''', '''CAP''') is a [[regulatory protein]] in [[bacteria]]. |
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'''cAMP receptor protein''' (in short '''CRP''', also known as '''catabolite gene activator protein''' (in short '''CAP''')) is a [[regulatory protein]] in [[bacteria]]. This [[protein]] binds [[Cyclic adenosine monophosphate|cAMP]], which causes a conformational change that allows the protein to bind to tightly to a specific DNA sequence in the [[promoter]]s of the genes it controls.<ref>{{cite journal |author=Harman JG |title=Allosteric regulation of the cAMP receptor protein |journal=Biochim. Biophys. Acta |volume=1547 |issue=1 |pages=1–17 |year=2001 |pmid=11343786}}</ref> The genes regulated by this protein are mostly involved in energy metabolism, such as [[galactose]], [[citrate]], or the [[PEP group translocation]] system.<ref>{{cite journal |author=Weickert MJ, Adhya S |title=The galactose regulon of Escherichia coli |journal=Mol. Microbiol. |volume=10 |issue=2 |pages=245–51 |year=1993 |pmid=7934815 |doi=10.1111/j.1365-2958.1993.tb01950.x}}</ref><ref>{{cite journal |author=Bott M |title=Anaerobic citrate metabolism and its regulation in enterobacteria |journal=Arch. Microbiol. |volume=167 |issue=2-3 |pages=78–88 |year=1997 |pmid=9133329 |doi=10.1007/s002030050419}}</ref> |
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== |
==Protein== |
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CRP [[protein]] binds [[cyclic adenosine monophosphate]] (cAMP), which causes a conformational change that allows CRP to bind tightly to a specific [[DNA]] site in the [[promoter (biology)|promoters]] of the genes it controls.<ref name=Busby>{{cite journal |author=Busby S., [[Richard H. Ebright|Ebright]] RH. |title=Transcription activation by catabolite activator protein (CAP) |journal=J. Mol. Biol. |volume=293 |pages=199–213 |year=1999 |pmid=10550204 |doi=10.1006/jmbi.1999.3161 |issue=2}}</ref><ref name=Lawson>{{cite journal |vauthors=Lawson CL, Swigon D, Murakami KS, Darst SA, Berman HM, Ebright RH |title=Catabolite activator protein: DNA binding and transcription activation |journal=Curr. Opin. Struct. Biol. |volume=14 |pages=10–20 |year=2004 |pmid=15102444 |doi=10.1016/j.sbi.2004.01.012 |issue=1 |pmc=2765107}}</ref> CRP then activates transcription through direct protein–protein interactions with [[RNA polymerase]].<ref name=Busby/><ref name=Lawson/> |
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{{reflist}} |
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The genes regulated by CRP are mostly involved in energy metabolism, such as [[galactose]], [[citrate]], or the [[PEP group translocation]] system.<ref>{{cite journal |vauthors=Weickert MJ, Adhya S |title=The galactose regulon of Escherichia coli |journal=Mol. Microbiol. |volume=10 |issue=2 |pages=245–51 |year=1993 |pmid=7934815 |doi=10.1111/j.1365-2958.1993.tb01950.x|s2cid=6872903 |url=https://zenodo.org/record/1230615 }}</ref><ref>{{cite journal |author=Bott M |title=Anaerobic citrate metabolism and its regulation in enterobacteria |journal=Arch. Microbiol. |volume=167 |issue=2–3 |pages=78–88 |year=1997 |pmid=9133329 |doi=10.1007/s002030050419|s2cid=22913073 }}</ref> In ''[[Escherichia coli]]'', CRP can regulate the transcription of more than 100 genes.<ref>{{Cite journal |last=Fic |first=E. |last2=Bonarek |first2=P. |last3=Gorecki |first3=A. |last4=Kedracka-Krok |first4=S. |last5=Mikolajczak |first5=J. |last6=Polit |first6=A. |last7=Tworzydlo |first7=M. |last8=Dziedzicka-Wasylewska |first8=M. |last9=Wasylewski |first9=Z. |date=2008-11-25 |title=cAMP Receptor Protein from Escherichia coli as a Model of Signal Transduction in Proteins – A Review |url=https://karger.com/mmb/article/17/1/1/196806/cAMP-Receptor-Protein-from-Escherichia-coli-as-a |journal=Journal of Molecular Microbiology and Biotechnology |volume=17 |issue=1 |pages=1–11 |doi=10.1159/000178014 |issn=1464-1801}}</ref> |
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==External links== |
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[http://www.mun.ca/biochem/courses/4103/topics/CRP.html crystal structure of CRP and binding site properties] |
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The signal to activate CRP is the binding of cyclic AMP. Binding of cAMP to CRP leads to a long-distance signal transduction from the [[N-terminal]] cAMP-binding domain to the [[C-terminal]] domain of the protein, which is responsible for interaction with specific sequences of DNA.<ref>{{Cite journal |
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| ⚫ | |||
| last1 = Popovych | first1 = N. |
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| last2 = Tzeng | first2 = S. -R. |
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| last3 = Tonelli | first3 = M. |
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| last4 = Ebright | first4 = R. H. |
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| last5 = Kalodimos | first5 = C. G. |
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| title = Structural basis for cAMP-mediated allosteric control of the catabolite activator protein |
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| doi = 10.1073/pnas.0900595106 |
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| journal = Proceedings of the National Academy of Sciences |
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| volume = 106 |
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| issue = 17 |
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| pages = 6927–6932 |
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| year = 2009 |
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| pmid = 19359484 |
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| pmc =2678429 |
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| doi-access = free |
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}}</ref> |
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At "Class I" CRP-dependent promoters, CRP binds to a DNA site located upstream of core promoter elements and activates transcription through protein–protein interactions between "activating region 1" of CRP and the C-terminal domain of [[RNA polymerase]] alpha subunit.<ref name=Busby/><ref name=Lawson/><ref>{{Cite journal |
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{{bacteria-stub}} |
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| last1 = Hudson | first1 = B. P. |
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{{protein-stub}} |
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| last2 = Quispe | first2 = J. |
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| last3 = Lara-Gonzalez | first3 = S. |
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| last4 = Kim | first4 = Y. |
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| last5 = Berman | first5 = H. M. |
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| last6 = Arnold | first6 = E. |
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| last7 = Ebright | first7 = R. H. |
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| last8 = Lawson | first8 = C. L. |
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| doi = 10.1073/pnas.0908782106 |
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| title = Three-dimensional EM structure of an intact activator-dependent transcription initiation complex |
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| journal = Proceedings of the National Academy of Sciences |
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| volume = 106 |
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| issue = 47 |
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| pages = 19830–19835 |
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| year = 2009 |
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| pmid = 19903881 |
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| pmc =2775702 |
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| doi-access = free |
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}}</ref> At "Class II" CRP-dependent promoters, CRP binds to a DNA site that overlaps the promoter -35 element and activates transcription through two sets of protein–protein interactions: (1) an interaction between "activating region 1" of CRP and the C-terminal domain of [[RNA polymerase]] alpha subunit, and (2) an interaction between "activating region 2" of CRP and the N-terminal domain of [[RNA polymerase]] alpha subunit.<ref name=Busby/><ref name=Lawson/> At "Class III" CRP-dependent promoters, CRP functions together with one or more "[[co-activator]]" proteins.<ref name=Busby/><ref name=Lawson/> |
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At most CRP-dependent promoters, CRP activates transcription primarily or exclusively through a "recruitment" mechanism, in which protein–protein interactions between CRP and [[RNA polymerase]] assist binding of [[RNA polymerase]] to the promoter.<ref name=Busby/> |
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==References== |
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{{Reflist}} |
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{{DEFAULTSORT:cAMP Receptor Protein}} |
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| ⚫ | |||
Latest revision as of 19:37, 9 November 2024
| CAMP receptor protein | |||||||
|---|---|---|---|---|---|---|---|
 Structure of the E. coli Cyclic AMP Receptor Protein. | |||||||
| Identifiers | |||||||
| Symbol | CRP | ||||||
| Alt. symbols | CAP | ||||||
| NCBI gene | 947867 | ||||||
| PDB | 1I5Z | ||||||
| RefSeq | NP_417816.1 | ||||||
| UniProt | P0ACJ8 | ||||||
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cAMP receptor protein (CRP; also known as catabolite activator protein, CAP) is a regulatory protein in bacteria.
Protein
[edit]CRP protein binds cyclic adenosine monophosphate (cAMP), which causes a conformational change that allows CRP to bind tightly to a specific DNA site in the promoters of the genes it controls.[1][2] CRP then activates transcription through direct protein–protein interactions with RNA polymerase.[1][2]
The genes regulated by CRP are mostly involved in energy metabolism, such as galactose, citrate, or the PEP group translocation system.[3][4] In Escherichia coli, CRP can regulate the transcription of more than 100 genes.[5]
The signal to activate CRP is the binding of cyclic AMP. Binding of cAMP to CRP leads to a long-distance signal transduction from the N-terminal cAMP-binding domain to the C-terminal domain of the protein, which is responsible for interaction with specific sequences of DNA.[6]
At "Class I" CRP-dependent promoters, CRP binds to a DNA site located upstream of core promoter elements and activates transcription through protein–protein interactions between "activating region 1" of CRP and the C-terminal domain of RNA polymerase alpha subunit.[1][2][7] At "Class II" CRP-dependent promoters, CRP binds to a DNA site that overlaps the promoter -35 element and activates transcription through two sets of protein–protein interactions: (1) an interaction between "activating region 1" of CRP and the C-terminal domain of RNA polymerase alpha subunit, and (2) an interaction between "activating region 2" of CRP and the N-terminal domain of RNA polymerase alpha subunit.[1][2] At "Class III" CRP-dependent promoters, CRP functions together with one or more "co-activator" proteins.[1][2]
At most CRP-dependent promoters, CRP activates transcription primarily or exclusively through a "recruitment" mechanism, in which protein–protein interactions between CRP and RNA polymerase assist binding of RNA polymerase to the promoter.[1]
References
[edit]- ^ a b c d e f Busby S., Ebright RH. (1999). "Transcription activation by catabolite activator protein (CAP)". J. Mol. Biol. 293 (2): 199–213. doi:10.1006/jmbi.1999.3161. PMID 10550204.
- ^ a b c d e Lawson CL, Swigon D, Murakami KS, Darst SA, Berman HM, Ebright RH (2004). "Catabolite activator protein: DNA binding and transcription activation". Curr. Opin. Struct. Biol. 14 (1): 10–20. doi:10.1016/j.sbi.2004.01.012. PMC 2765107. PMID 15102444.
- ^ Weickert MJ, Adhya S (1993). "The galactose regulon of Escherichia coli". Mol. Microbiol. 10 (2): 245–51. doi:10.1111/j.1365-2958.1993.tb01950.x. PMID 7934815. S2CID 6872903.
- ^ Bott M (1997). "Anaerobic citrate metabolism and its regulation in enterobacteria". Arch. Microbiol. 167 (2–3): 78–88. doi:10.1007/s002030050419. PMID 9133329. S2CID 22913073.
- ^ Fic, E.; Bonarek, P.; Gorecki, A.; Kedracka-Krok, S.; Mikolajczak, J.; Polit, A.; Tworzydlo, M.; Dziedzicka-Wasylewska, M.; Wasylewski, Z. (2008-11-25). "cAMP Receptor Protein from Escherichia coli as a Model of Signal Transduction in Proteins – A Review". Journal of Molecular Microbiology and Biotechnology. 17 (1): 1–11. doi:10.1159/000178014. ISSN 1464-1801.
- ^ Popovych, N.; Tzeng, S. -R.; Tonelli, M.; Ebright, R. H.; Kalodimos, C. G. (2009). "Structural basis for cAMP-mediated allosteric control of the catabolite activator protein". Proceedings of the National Academy of Sciences. 106 (17): 6927–6932. doi:10.1073/pnas.0900595106. PMC 2678429. PMID 19359484.
- ^ Hudson, B. P.; Quispe, J.; Lara-Gonzalez, S.; Kim, Y.; Berman, H. M.; Arnold, E.; Ebright, R. H.; Lawson, C. L. (2009). "Three-dimensional EM structure of an intact activator-dependent transcription initiation complex". Proceedings of the National Academy of Sciences. 106 (47): 19830–19835. doi:10.1073/pnas.0908782106. PMC 2775702. PMID 19903881.