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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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== '''Mary Osborn''' (born 1940)<ref name=":0" /> is an award-winning English cell biologist who, until she stopped running an active laboratory in 2005,<ref name=":1" /> was on the scientific staff at the Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.<ref name=":1" /> Osborn established two of the most vital techniques in use by cell biologists. She pioneered both molecular weight determination of proteins using SDS PAGE<ref name=":4" /> and immunofluorescence microscopy.<ref name=":5" /> She used the immunofluorescence microscopy method to work out the details of the eukaryotic cytoskeleton, and showed that small differences in the intermediate filament constituents enabled her to distinguish types of cell as well as normal versus cancer cells. Mary Osborn has been a prominent spokesperson for women in science. <ref name=":2" /> She has received the Meyenberg Prize for Cancer Research in 1987 and the Lóreal / UNESCO Prize for Women in Science in 2002 among other awards and honors.<ref name=":2" /> == |
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Contents |
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== Education == |
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1 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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== 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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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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3 Support for Women in Science |
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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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5 References |
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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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'''Early Life and Education''' |
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American Academy Announces 2004 Fellows and Foreign Honorary Members |
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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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Osborn was born in [[Darlington|Darlington, UK]]<ref name=":0">F. M. Watt. (2004) "Mary Osborn" ''Journal of Cell Science'' '''117'''(8):1255-1256.</ref> on December 16, 1940.<ref name=":6">{{Cite web|url=https://prabook.com/web/mary.osborn/131457|title=Mary Osborn|last=Osborn|first=Mary|date=2018|website=Prabook is a registered trademark of World Biographical Encyclopedia, Inc. |
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Version 2.0.21.5829 2018|archive-url=|archive-date=|dead-url=|access-date=}}</ref> Osborn completed high school education at [[Cheltenham Ladies' College]] and university education at [[Newnham College, Cambridge|Newnham College]], Cambridge University where she was graduated in Mathematics and Physics in 1962.<ref name=":0" /> She received a masters in biophysics at [[Pennsylvania State University]] in 1963 . Her PhD on [[mutagenesis]] in [[Nonsense mutation|nonsense mutations]] in bacteria was awarded by Pennsylvania State University in 1972.<ref name=":1">{{Cite web|url=https://www.uni-goettingen.de/de/prof.+mary+osborn%2C+mpi+for+biophysical+chemistry%2C+g%C3%B6ttingen/361895.html|title=Mary Osborn|last=Osborn|first=Mary|date=2018|website=Goettingen Max Planck Institute for Biophysical Chemistry|archive-url=|archive-date=|dead-url=|access-date=}}</ref> |
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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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'''Research''' '''Career''' |
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== Selected Works == |
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Mary Osborn carried out postdoctoral research in the laboratory of [[James Watson]] at [[Harvard University]].<ref name=":1" /> Then she conducted research at the Laboratory of Molecular Biology, [[Cambridge]], UK for three years before moving to the [[Cold Spring Harbor Laboratory]] for two and a half years.<ref name=":0" /> Osborn had married her husband, Klaus Weber, on July 14, 1972.<ref name=":6" /> Weber and Osborn moved to the [[University of Göttingen|Göttingen]] [[Max Planck Institute for Biophysical Chemistry]] in 1975.<ref name=":0" /> in 1989, she was appointed an honorary professor at University of Göttingen.<ref name=":1" /> |
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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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Mary Osborn and [[Klaus Weber]] wrote a classic paper in biochemistry on determination of the molecular weight of a protein via [[SDS-PAGE|SDS polyacrylamide gel electrophoresis]], published in 1969 in ''[[Journal of Biological Chemistry]]''.<ref name=":3">Nicole Kresge, Robert Simoni, and Robert Hill. (2006) "Classics. A paper in a series reprinted to celebrate the centennial of the JBC in 2005. SDS PAGE to determine the molecular weight of proteins: the work of Klaus Weber and Mary Osborn." ''Journal of Biological Chemistry '''281''' (24): e19.'' </ref><ref name=":4">Klaus Weber and Mary Osborn. (1969) "The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis" ''Journal of Biological Chemistry'' '''213''' (16): 4406-4412.</ref> They knew that in 1967 Shapiro, Vinuela, and Maisel had shown that electrophoresis of proteins along with Sodium Dodecyl Sulfate (SDS) in polyacrylamide gels (PAGE) could separate the tested polypeptide chains by molecular weight.<ref>AL Shapiro, E. Vinuela, and JV Maizel., Jr. (1967) "Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels." ''Biochem. Biophys. Res. Commun.'' '''28:''' 815–820,</ref> To see if this method applied to proteins of various sizes and shapes, Osborn and Weber took 40 known proteins, including globular and filamentous proteins, analyzed them via SDS PAGE, and plotted the logarithms of their molecular weights against their electrophoretic mobilities.<ref name=":3" /> The results showed convincingly that “the good resolution and the fact that an estimate of the molecular weight can be obtained within a day, together with the small amount of protein needed, makes the method strongly competitive with others commonly employed.”<ref name=":4" /> This method has been used extensively by biochemists in all kinds of studies involving protein purification and identification as part of the process. |
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Later, Osborn and Weber pioneered fluorescent antibody staining of cellular substructures, a major technique called indirect [[Immunofluorescence|immunofluorescence microscopy]].<ref name=":2">Silvia Sanides. (2004) "Cell Biologist Multitasks for Women" ''The Scientist,'' March 15. </ref> In developing the method, they tagged microtubules with specific antibodies, then used fluorescently-tagged secondary antibodies (antibodies to the first set of antibodies) to light up the locations of the microtubules in cells.<ref name=":3" /> They developed new antibodies against proteins of the microtubules, intermediate filaments, and microfilaments to use as reagents in examining many types of cells.<ref name=":7">“Genome Biology: Women in Science.” (2012) Geno''me Biology'' '''13''': 148-154''.'' doi:10.1186/gb-2012-13-3-148.</ref> Klaus and Osborn used this method to study elements of the [[cytoskeleton]] of [[Eukaryote|eukaryotic cells]] in two dimensions and three dimensions.<ref name=":5">Mary Osborn, Werner Franke, and Klaus Weber, (1977) "Visualization of a system of filaments 7-10nm thick in cultured cells of an epithelioid line (Pt K2) by immunofluorescence microscopy" ''Proceedings of the National Academy of Sciences'' '''74''' (6):2490-2494. </ref> Osborn has studied microtubules, [[Intermediate filament|intermediate filaments]], microfilaments, and other proteins that can associate with these structures. In the course of observing [[Microfilament|microfilaments,]] by 1981 Osborn and Klaus had shown conclusively intermediate filaments in different types of cells are different but related, and they can be distinguished using immunofluorescence.<ref>M. Altmannsberger, M. Osborn, A. Schauer, and K. Weber. (1981) “Antibodies to different intermediate filament proteins, cell type-specific markers on paraffin- embedded human tissues.” ''Lab. Invest''. '''45''', 427-434.</ref> Soon thereafter, in 1982, the laboratory showed that many tumors differ from their matching normal tissue in the protein details of intermediate filaments as shown by immunofluorescence. <ref>M. Altmannsberger, M. Osborn, K. Weber, and A. Schauer. (1982) “Expression of intermediate filaments in different human epithelial and mesenchymal tumors.” ''Path. Res. Pract.'' '''175''', 227-237.</ref> They also found that intermediate filament composition was tumor-specific.<ref name=":7" /> Osborn and Weber have pioneered the diagnostic classification of tumor types using specific cytoskeletal elements determined via immunofluorescence microscopy. Their methods have been applied in numerous clinical studies of [[muscular dystrophy]] and [[cancer]]. <ref name=":2" /> |
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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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'''Support of Women in Science''' |
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When Mary Osborn returned to Europe after years in the USA, she was surprised to find that European science had not opened its doors to women as she had experienced in America. She was quoted in an article in ''Science'' in 1994 to the effect that women's role in Germany was still "kinder, küche, kirche" (children, kitchen, church.)<ref>Peter Aldhous, (1994) “News: Germany. The Backbreaking Work of Scientist Homemakers.” ''Science'''''263''' (5152):1475-1480.</ref> In 1992, she had written a protest letter in response to a letter in ''[[Nature (journal)|Nature]]'' that had claimed child care issues were chiefly responsible for the leaky pipeline for [[Women in STEM fields|women in science]], not discrimination.<ref name=":3" /> She noted in 2012 that there was still a leaky pipeline for women scientists in Germany.<ref name=":7" /> As a woman without children who had experienced no gender discrimination early in her career but had seen differential treatment of men and women in science later, she did not find this argument convincing, and she was appalled to find out that Europe had collected little or no data on rates of success of women in science. Partly because Osborn objected to this situation, the EC appointed her co-chair of a working group to investigate the status of European women scientists and scientists in training and in employment and to prepare a report.<ref name=":2" /> The outcome was the European Technology Assessment Network (ETAN) Report on Women in Science, published in 2006, which identified a number of well-substantiated reasons why women dropped out of science and served as a blueprint for Europeans who wished to fix this problem.<ref name=":2" /><ref name=":3" /> She has given a great deal of thought to how women are taught to act as they grow up and how that may impact their career decisions. In an interview in 2004, Osborn said, "In deciding whether to accept new challenges a remark by Diane Britten some years ago in ''The Times'' has proved very helpful: “When asked to do something women tend to say `Why me?' Men say `Why not me?' I have learned to say `Why not me?<nowiki>'''</nowiki><ref name=":0" /> Summing up her advice to those in charge of sciences in universities and industry, she said in 2012, "Above all one has to get the argument across that it is wasteful, expensive and unfair to educate and train large numbers of female scientists and then not use their talents in the job market or provide equal access to the top jobs."<ref name=":7" /> |
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'''Awards and honors'''<ref>{{Cite web|url=http://www.academia-net.org/profil/prof-dr-dr-h-c-mary-osborn/1133992|title=Mary Osborn|last=Academia Net|first=|date=2018|website=Academia Net|archive-url=|archive-date=|dead-url=|access-date=}}</ref> |
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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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* 1979 Elected member, European Molecular Biology Organisation |
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*1987 Meyenburg Prize for Cancer Research |
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*1995 Elected member, Academia Europaea |
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*1997 Doctorate honoris causa, Pomeranian Medical Academy, Szczecin, Poland |
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*1998 Carl Zeiss Prize, German Society Cell Biology, (shared with Klaus Weber) |
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*1998 Helena Rubenstein / UNESCO Prize for Women in Science (UK) |
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*2002 Lóreal / UNESCO Prize for Women in Science |
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*2005 Outstanding Science Alumni Award, Pennsylvania State University, USA |
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*2007 Dorothea Schlözer Medal, University of Göttingen, Germany |
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'''References''' |
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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.