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{{User sandbox|LLMHoopes|plain=sandbox1|selectskin=|afc=|MaryOsborn=}} |
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Linda Randall is a Professor Emerita of Biochemistry and Wurdack Chair Emerita of Biological Chemistry at University of Missouri.<ref name=":0">{{Cite web|url=https://biochem.missouri.edu/faculty/faculty-members/randalll/index.php|title=Linda Randall|last=|first=|date=|website=University of Missouri|archive-url=|archive-date=|access-date=December 4, 2018}}</ref> Her research has shown unexpected and complex details of the movement of newly made proteins from the cytosol across membranes into organelles of the cell. In particular, she found that the entire protein was kept unfolded by association with a chaperone and not just directed to cross membranes by its terminal leader sequence.<ref name=":1">{{Cite web|url=http://www.nasonline.org/member-directory/members/3003916.html|title=Linda Randall|last=|first=|date=|website=National Academy of Sciences|archive-url=|archive-date=|access-date=December 4, 2018}}</ref> In 1997, she was elected to the National Academy of Sciences of the USA because of the excellence of this work. She has received a number of other honors and awards.<ref name=":1" /> |
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== Education == |
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=== '''Early life and education''' === |
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Linda Randall received the BS at Colorado State University in Zoology and the PhD at University of Wisconsin in Molecular Biology.<ref name=":0" /> |
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Christine Jacobs-Wagner grew up in [[Belgium]] in a town near [[Liège|Liege]].<ref name=":1">{{Cite web|url=http://jcb.rupress.org/content/189/3/390|title=Christine Jacobs-Wagner: Drawing the bacterial organizational chart|last=|first=|date=|website=Journal of Cell Biology|archive-url=|archive-date=|dead-url=|access-date=October 21, 2018}}</ref> She thought of becoming a [[Cycling|cyclist]]<ref name=":1" /> or a [[badminton]] Olympian,<ref>{{Cite web|url=https://www.the-scientist.com/uncategorized/a-fierce-competitor-45291|title=A Fierce Competitor|last=Hopkin|first=Karen|date=April 1, 2008|website=The Scientist|archive-url=|archive-date=|dead-url=|access-date=October 22, 2018}}</ref> but was undecided about a career through high school.<ref name=":1" /> Christine Jacobs-Wagner received her BS degree in [[biochemistry]] from [[University of Liège|University of Liege]].<ref name=":0">{{Cite web|url=http://blavatnikawards.org/honorees/profile/christine-jacobs-wagner/|title=Blavatnik Awards Christine Jacobs-Wagner|last=|first=|date=|website=Blavatnik Foundation|archive-url=|archive-date=|dead-url=|access-date=October 20, 2018}}</ref> She also received her MS in 1991 and the PhD in 1996 from University of Liege in Belgium in the field of Biochemistry.<ref name=":2" /> She then went to work with [[Lucy Shapiro]] at [[Stanford University School of Medicine|Stanford Medical School]] on a fellowship from the [[European Molecular Biology Organization|European molecular Biology Organization]]. where she studied ''[[Caulobacter crescentus|Caulobacter]]'', a bacterium with a [[flagellum]] on one end and a stalk on the other end, beginning her fascination with how bacterial cells can become [[Asymmetry|asymmetrical]].<ref name=":1" /> From 2004 to 2013, she did research in [[Newcastle upon Tyne]] in the United Kingdom.<ref name=":2">{{Cite web|url=https://medicine.yale.edu/micropath/people/christine_jacobs-wagner.profile|title=Christine Jacobs-Wagner|last=|first=|date=|website=Yale Medical School|archive-url=|archive-date=|dead-url=|access-date=October 20, 2018}}</ref> <ref name=":0" /> |
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== Academic Research Career == |
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Linda Randall was a professor at University of Uppsala, Sweden for eight years and joined the faculty at Washington State University in 1981.<ref>{{Cite web|url=https://s3.wp.wsu.edu/uploads/sites/9/2016/09/WSUchemNewsletter-Summer1997ocr.pdf|title=Biochemists Elected to the National Academy of Sciences|last=|first=|date=1997|website=Washington State University Biochemistry Department|archive-url=|archive-date=|access-date=December 4, 2018}}</ref> She was a professor at Washington State University for twenty years, but in 2000, she received an attractive offer from University of Missouri and moved there along with her husband.<ref name=":2">{{Cite web|url=https://lmtribune.com/education/departing-profs-have-harsh-words-for-wsu-research-team-leaders/article_d030c0b4-dfc8-58ed-8e9b-7a5829f4f839.html|title=Departing Professors Have Harsh Words for WSU|last=Smith|first=Debra|date=September 22, 2000|website=The Lewiston Tribune|archive-url=|archive-date=|access-date=December 4, 2018}}</ref> She and her husband, Gerald Hazelbauer, chair of biochemistry, gave an interview to ''The Lewiston Tribune'' saying that they had decided to leave the Pullman campus partly due to the inability of WSU to promote academic excellence and set a high standard for student behavior. The excessive drinking and wild behavior was their main issue.<ref name=":2" /> The two professors took over three quarters of a million dollars in federal research funding with them to Missouri.<ref name=":2" /> |
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As of 2018, Jacobs-Wagner holds an endowed chair in Yale Medical School and is director of their Microbial Institute.<ref name=":1" /><ref name=":2" /> |
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Linda Randall showed the mechanism of protein export in the bacterium ''Escherichia coli''.<ref name=":3">{{Cite web|url=https://biochem.missouri.edu/faculty/faculty-members/randalll/index.php|title=Linda Randall|last=|first=|date=|website=University of Missouri Biochemistry Department|archive-url=|archive-date=|access-date=December 4, 2018}}</ref> It is not an easy task to move a protein folded into its tertiary and quaternary structures through a membrane, but many proteins must be moved from their synthesis site in the cytosol to other places in the cell that are separated from the cytosol by membranes. It was known that proteins that move across membranes are synthesized with a particular leader peptide and it was once thought that any transport process would focus on that leader peptide.<ref name=":1" /> However, Randall’s laboratory showed that the whole length of nascent proteins are kept in their unfolded state by associating them with a chaperone protein to facilitate their transfer to another compartment in the cell bounded by a membrane.<ref name=":1" /> The role of the SecB chaperone and its ATPase partner SecA in assisting newly made polypeptides to cross membranes was worked out in her laboratory.<ref name=":3" /> Her development of a system to study membrane translocation in the test tube has been important in her own research and that of others.<ref name=":3" /> |
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=== '''Research''' === |
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Christine Jacobs-Wagner's major breakthrough has been the discovery that the tiny cells of bacteria such as ''Caulobacter,'' ''[[Escherichia coli]]'', and ''[[Borrelia]]'' are not simply bags of biochemicals but instead program the locations of their protein components via their regulatory systems.<ref name=":1" /> She also discovered the protein [[crescentin]] which forms bacterial [[Intermediate filament|intermediate filaments]], structures once thought to occur only in [[Eukaryote|eukaryotic]] cells.<ref name=":1" /> The current focus of her laboratory's work is to discover regulation of the times and places for critical components of the [[DNA replication]] and [[cell division]] processes so that proliferation control can be understood.<ref name=":1" /> |
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== Honors and Awards == |
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National Academy of Sciences, 1997<ref name=":1" /> |
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American Academy of Microbiology<ref name=":3" /> |
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* National Academy of Sciences (2015)<ref>{{Cite web|url=http://www.nasonline.org/member-directory/members/20036037.html|title=Christine Jacobs-Wagner|last=|first=|date=|website=National Academy of Sciences|archive-url=|archive-date=|dead-url=|access-date=October 20, 2018}}</ref> |
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*[[Eli Lilly Award in Biological Chemistry|Eli Lilly Award]] American Society of Microbiology (2011)<ref name=":0" /> |
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* WALS lecture [[National Institutes of Health|National Institute of Health]] (2009)<ref name=":0" /> |
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*[[Elizabeth McCoy (microbiologist)|Elizabeth McCoy]] Lecture<ref name=":0" /> |
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* Finalist, Blatvanik Award for Young Scientists [[New York Academy of Sciences]] (2008)<ref name=":0" /> |
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* Women in Cell Biology [[WICB Junior and Senior Awards|WICB Junior and Senior Award]] by [[American Society for Cell Biology|American Society of Cell Biology]] (2007)<ref>{{Cite web|url=https://www.ascb.org/wicb-awards/|title=Women in Cell Biology Awards (Amer Soc for Cell Biol)|last=|first=|date=|website=American Society for Cell Biology|archive-url=|archive-date=|dead-url=|access-date=October 22, 2018}}</ref> |
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* Pew Scholarship Award in the Biomedical Sciences [[The Pew Charitable Trusts|PEW Charitable Trust]] (2003)<ref name=":0" /> |
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* Grand Prize Winner of the Young Scientist Award GE & Science (1997)<ref name=":0" /> |
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American Academy of Arts and Sciences, 1984<ref>{{Cite web|url=https://www.amacad.org/content/news/pressReleases.aspx?pr=59 |
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| ⚫ | |||
American Academy Announces 2004 Fellows and Foreign Honorary Members |
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MT Cabeen, C Jacobs-Wagner 2005 “Bacterial Cell Shape” ''Nature Reviews Microbiology'' '''3''' (8):601-610. |
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4/30/2004|title=American Academy of Arts and Sciences Announces 2004 Fellows and Foreign Hnorary Members|last=|first=|date=April 30, 2004|website=|archive-url=|archive-date=|access-date=December 4, 2018}}</ref> |
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Fellow of American Association for the Advancement of Science<ref name=":3" /> |
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O. Sliusarenko, J Heinritz, T Emonet, and C Jacobs-Wagner 2011 “High-throughput, suppixel precision analysis of bacterial morphogenesis and spatio-temporal dynamics.” M''olecular Microbiology'' '''80''' (3):612-627. |
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Eli Lilly Award in Microbiology or Immunology (American Society for Microbiology)<ref>{{Cite web|url=https://www.asm.org/index.php/component/content/article/140-awards-a-grants/past-laureates/7791-eli-lilly-and-company-elanco-research-award-past-laureates|title=Eli Lilly and Company Elanco Research Award Past Laureates|last=|first=|date=|website=American Society for Microbiology|archive-url=|archive-date=|access-date=December 4, 2018}}</ref> |
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N Ausmees, JR Kuhn, and C Jacobs-Wagner (2003) “The bacterial cytoskeleton: an intermediate filament-like function in cell shape“ ''Cell'' '''115''' (6): 705-713. |
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PM Llopis, AF Jackson, O Sliusarenko, I Surovtsev, J Heinritz, T Emonet…C Jacobs-Wagner (2010) “Spatial organization of the flow of genetic information in bacteria“ ''Nature'' '''466''' (7302):77-81. |
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Bariya P, Randall LL. (2018). “Co-assembly of SecYEG and SecA fully restores the properties of the native translocon.” ''J Bacteriol''. 2018 Oct 1. doi: 10.1128 JB.00493-18 Epub ahead of print. |
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G Laloux and C Jacobs-Wagner (2014) “How do bacteria localize proteins to the cell pole? ''J Cell Science'' 127: 11-19. doi:10.1242/jcs.138328 |
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M Cabeen and C Jacobs-Wagner (2010) “The bacterial cytoskeleton” ''Annu Rev Genetics'' '''44''': 365-382. |
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Findik BT, Smith VF, Randall LL. (2018). “Penetration into membrane of amino-terminal region of SecA when associated with SecYEG in active complexes.” ''Protein Sci''. '''27'''(3):681-691. doi: 10.1002/pro.3362. |
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=== '''References''' === |
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Suo Y, Hardy SJS, Randall LL. (2015). “The basis of asymmetry in the SecA:SecB complex.” ''J Mol Biol''. '''427'''(4):887-900. doi: 10.1016/j.jmb.2014.12.008. [PubMed] |
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Mao C, Cheadle CE, Hardy SJ, Lilly AA, Suo Y, Sanganna Gari RR, King GM, Randall LL. (2013). “Stoichiometry of SecYEG in the active translocase of ''Escherichia coli'' varies with precursor species.” ''Proc Natl Acad Sci U S A''. '''110'''(29):11815-20. doi: 10.1073/pnas.1303289110. [PubMed] |
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Sanganna Gari RR, Frey NC, Mao C, Randall LL, King GM. (2013). “Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations.” ''J Biol Chem''. '''288'''(23):16848-54. doi: 10.1074/jbc.M113.471870. [PubMed] |
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Suo Y, Hardy SJ, Randall LL. (2011). “Orientation of SecA and SecB in complex, derived from disulfide cross-linking.” ''J Bacteriol''. '''193'''(1):190-6. doi: 10.1128/JB.00975-10. [PubMed] |
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Randall LL, Henzl MT. (2010). “Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA.” ''Protein Sci''. '''19'''(6):1173-9. doi: 10.1002/pro.392. [PubMed] |
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Crane JM, Lilly AA, '''R'''andall LL. (2010). “Characterization of interactions between proteins using site-directed spin labeling and electron paramagnetic resonance spectroscopy.” ''Methods Mol Biol''. '''619''':173-90. doi: 10.1007/978-1-60327-412-8_11. [PubMed] |
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Lilly AA, Crane JM, Randall LL. (2009). “Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands.” ''Protein Sci''. '''18'''(9):1860-8. doi: 10.1002/pro.197. [PubMed] |
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Randall, L.L. and Hardy, S.J.S. (1995) “High selectivity with low specificity: how SecB has solved the paradox of chaperone binding.” ''Trends in Biochem Sci'' '''20''':65-69. |
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DOI:<nowiki>https://doi.org/10.1016/S0968-0004(00)88959-8</nowiki> |
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<br /> |
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Latest revision as of 15:25, 6 June 2022
Linda Randall is a Professor Emerita of Biochemistry and Wurdack Chair Emerita of Biological Chemistry at University of Missouri.[1] Her research has shown unexpected and complex details of the movement of newly made proteins from the cytosol across membranes into organelles of the cell. In particular, she found that the entire protein was kept unfolded by association with a chaperone and not just directed to cross membranes by its terminal leader sequence.[2] In 1997, she was elected to the National Academy of Sciences of the USA because of the excellence of this work. She has received a number of other honors and awards.[2]
Education
[edit]Linda Randall received the BS at Colorado State University in Zoology and the PhD at University of Wisconsin in Molecular Biology.[1]
Academic Research Career
[edit]Linda Randall was a professor at University of Uppsala, Sweden for eight years and joined the faculty at Washington State University in 1981.[3] She was a professor at Washington State University for twenty years, but in 2000, she received an attractive offer from University of Missouri and moved there along with her husband.[4] She and her husband, Gerald Hazelbauer, chair of biochemistry, gave an interview to The Lewiston Tribune saying that they had decided to leave the Pullman campus partly due to the inability of WSU to promote academic excellence and set a high standard for student behavior. The excessive drinking and wild behavior was their main issue.[4] The two professors took over three quarters of a million dollars in federal research funding with them to Missouri.[4]
Linda Randall showed the mechanism of protein export in the bacterium Escherichia coli.[5] It is not an easy task to move a protein folded into its tertiary and quaternary structures through a membrane, but many proteins must be moved from their synthesis site in the cytosol to other places in the cell that are separated from the cytosol by membranes. It was known that proteins that move across membranes are synthesized with a particular leader peptide and it was once thought that any transport process would focus on that leader peptide.[2] However, Randall’s laboratory showed that the whole length of nascent proteins are kept in their unfolded state by associating them with a chaperone protein to facilitate their transfer to another compartment in the cell bounded by a membrane.[2] The role of the SecB chaperone and its ATPase partner SecA in assisting newly made polypeptides to cross membranes was worked out in her laboratory.[5] Her development of a system to study membrane translocation in the test tube has been important in her own research and that of others.[5]
Honors and Awards
[edit]National Academy of Sciences, 1997[2]
American Academy of Microbiology[5]
American Academy of Arts and Sciences, 1984[6]
Fellow of American Association for the Advancement of Science[5]
Eli Lilly Award in Microbiology or Immunology (American Society for Microbiology)[7]
Selected Works
[edit]Bariya P, Randall LL. (2018). “Co-assembly of SecYEG and SecA fully restores the properties of the native translocon.” J Bacteriol. 2018 Oct 1. doi: 10.1128 JB.00493-18 Epub ahead of print.
Findik BT, Smith VF, Randall LL. (2018). “Penetration into membrane of amino-terminal region of SecA when associated with SecYEG in active complexes.” Protein Sci. 27(3):681-691. doi: 10.1002/pro.3362.
Suo Y, Hardy SJS, Randall LL. (2015). “The basis of asymmetry in the SecA:SecB complex.” J Mol Biol. 427(4):887-900. doi: 10.1016/j.jmb.2014.12.008. [PubMed]
Mao C, Cheadle CE, Hardy SJ, Lilly AA, Suo Y, Sanganna Gari RR, King GM, Randall LL. (2013). “Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.” Proc Natl Acad Sci U S A. 110(29):11815-20. doi: 10.1073/pnas.1303289110. [PubMed]
Sanganna Gari RR, Frey NC, Mao C, Randall LL, King GM. (2013). “Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations.” J Biol Chem. 288(23):16848-54. doi: 10.1074/jbc.M113.471870. [PubMed]
Suo Y, Hardy SJ, Randall LL. (2011). “Orientation of SecA and SecB in complex, derived from disulfide cross-linking.” J Bacteriol. 193(1):190-6. doi: 10.1128/JB.00975-10. [PubMed]
Randall LL, Henzl MT. (2010). “Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA.” Protein Sci. 19(6):1173-9. doi: 10.1002/pro.392. [PubMed]
Crane JM, Lilly AA, Randall LL. (2010). “Characterization of interactions between proteins using site-directed spin labeling and electron paramagnetic resonance spectroscopy.” Methods Mol Biol. 619:173-90. doi: 10.1007/978-1-60327-412-8_11. [PubMed]
Lilly AA, Crane JM, Randall LL. (2009). “Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands.” Protein Sci. 18(9):1860-8. doi: 10.1002/pro.197. [PubMed]
Randall, L.L. and Hardy, S.J.S. (1995) “High selectivity with low specificity: how SecB has solved the paradox of chaperone binding.” Trends in Biochem Sci 20:65-69.
DOI:https://doi.org/10.1016/S0968-0004(00)88959-8
- ^ a b "Linda Randall". University of Missouri. Retrieved December 4, 2018.
- ^ a b c d e "Linda Randall". National Academy of Sciences. Retrieved December 4, 2018.
- ^ "Biochemists Elected to the National Academy of Sciences" (PDF). Washington State University Biochemistry Department. 1997. Retrieved December 4, 2018.
- ^ a b c Smith, Debra (September 22, 2000). "Departing Professors Have Harsh Words for WSU". The Lewiston Tribune. Retrieved December 4, 2018.
- ^ a b c d e "Linda Randall". University of Missouri Biochemistry Department. Retrieved December 4, 2018.
- ^ [https://www.amacad.org/content/news/pressReleases.aspx?pr=59
American Academy Announces 2004 Fellows and Foreign Honorary Members
4/30/2004 "American Academy of Arts and Sciences Announces 2004 Fellows and Foreign Hnorary Members"]. April 30, 2004. Retrieved December 4, 2018.
{{cite web}}: Check|url=value (help); line feed character in|url=at position 61 (help) - ^ "Eli Lilly and Company Elanco Research Award Past Laureates". American Society for Microbiology. Retrieved December 4, 2018.