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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" />
Victoria Lundblad is a professor whose work focuses on the genetic control of chromosome behavior in yeast.<ref name=":0">{{Cite web|url=https://www.bcm.edu/research/office-of-research/debakey-awards/recipients/lundblad-victoria|title=Lundblad Victoria J. PhD|last=|first=|date=|website=Baylor College of Medicine|archive-url=|archive-date=|dead-url=|access-date=October 30, 2018}}</ref> Many of her discoveries have concerned telomerase, the RNA-containing enzyme that completes the ends of chromosomes.<ref name=":0" />


== Early Life and Education ==
== Education ==
Linda Randall received the BS at Colorado State University in Zoology and the PhD at University of Wisconsin in Molecular Biology.<ref name=":0" />
Victoria Lundblad was born in the Bay Area of California to a biochemist and a school teacher.<ref name=":1">{{Cite web|url=http://www.nasonline.org/member-directory/members/20036008.html|title=Victoria Lundblad|last=|first=|date=|website=National Academy of Sciences|archive-url=|archive-date=|dead-url=|access-date=October 30, 2018}}</ref> Vicki Lundblad was involved in science experiments as early as junior high school, testing whether skin emitted substances that repelled mosquitoes.<ref name=":2">{{Cite web|url=https://www.rockefeller.edu/greengard-prize/recipients/lundblad/|title=Vicki Lundblad|last=Strauss|first=Evelyn|date=|website=Rockefeller University|archive-url=|archive-date=|dead-url=|access-date=October 30, 2018}}</ref> She then took up playing the cello and threw herself into music studies; arriving at University of California, Berkeley,<ref name=":1" /> she meant to major in mathematics and music.<ref name=":2" /> She narrowed it down to Mathematics, but later added Biology.<ref name=":1" />


== Academic Research Career ==
She pursued graduate education in biology at Harvard University, where she became Nancy Kleckner's first graduate student.<ref name=":1" /> At Harvard, she was excited by a lecture by Jack Szostak, Nobel laureate in 2016, about his work on telomeres with Elizabeth Blackburn.<ref name=":2" /> She began a postdoctoral fellowship in 1983, working with Jack Szostak on yeast with a defective telomerase that underwent early senescence.<ref name=":2" /> She continued her study of telomeres as a postdoctoral fellow in Elizabeth Blackburn's laboratory. In 1991, she joined the Genetics Department at Baylor College of Medicine.<ref name=":1" /> In 2004, she moved to the Salk Institute.<ref name=":1" />
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" />


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" />
== Research ==
In 1989, Lundblad identified a gene, named EST1,("ever shorter telomeres") in which telomeres are lost, and found that EST1 encoded a regulatory subunit of telomerase.<ref name=":2" /> Later, collaborating with Nobel laureate Tom Cech, she discovered the catalytic subunit of telomerase and identified it as a reverse transcriptase with associated RNA.<ref name=":1" />


== Honors and Awards ==
== Honors and Awards ==
1997 DeBakey Excellence in Research Award from Baylor University<ref name=":0" />
National Academy of Sciences, 1997<ref name=":1" />


2008 Pearl Mester Greengard Prize from Rockefeller University.<ref name=":2" />
American Academy of Microbiology<ref name=":3" />


American Academy of Arts and Sciences, 1984<ref>{{Cite web|url=https://www.amacad.org/content/news/pressReleases.aspx?pr=59
2015 National Academy of Sciences in Medical Genetics, Hematology, and Oncology
American Academy Announces 2004 Fellows and Foreign Honorary Members
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>


Fellow of American Association for the Advancement of Science<ref name=":3" />
Selected Works


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>
Nugent CI, Hughes TR, Lue NF, Lundblad V. Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance. Science. 1996 Oct 11;274(5285):249-52.


== Selected Works ==
Lundblad V, Wright WE. Telomeres and telomerase: a simple picture becomes complex. Cell. 1996 Nov 1;87(3):369-75.
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.


Virta-Pearlman V, Morris DK, Lundblad V. Est1 has the properties of a single-stranded telomere end-binding protein. Genes Dev. 1996 Dec 15;10(24):3094-104.


Lendvay TS, Morris DK, Sah J, Balasubramanian B, Lundblad V. Senescence mutants of Saccharomyces cerevisiae with a defect in telomere replication identify three additional EST genes. Genetics. 1996 Dec;144(4):1399-412.


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.  
Linger J, Hughes TR, Shevchenko A, Mann M, Lundblad V, Cech TR. Reverse transcriptase motifs in the catalytic subunit of telomerase. Science. 1997 Apr 25;276(5312):561-7.



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, '''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]



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:<nowiki>https://doi.org/10.1016/S0968-0004(00)88959-8</nowiki>
<br />

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

  1. ^ a b "Linda Randall". University of Missouri. Retrieved December 4, 2018.
  2. ^ a b c d e "Linda Randall". National Academy of Sciences. Retrieved December 4, 2018.
  3. ^ "Biochemists Elected to the National Academy of Sciences" (PDF). Washington State University Biochemistry Department. 1997. Retrieved December 4, 2018.
  4. ^ a b c Smith, Debra (September 22, 2000). "Departing Professors Have Harsh Words for WSU". The Lewiston Tribune. Retrieved December 4, 2018.
  5. ^ a b c d e "Linda Randall". University of Missouri Biochemistry Department. Retrieved December 4, 2018.
  6. ^ [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)
  7. ^ "Eli Lilly and Company Elanco Research Award Past Laureates". American Society for Microbiology. Retrieved December 4, 2018.