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Linda Randall is a Professor Emerita of Biochemistry and Wurdack Chair Emerita of Biological Chemistry at University of Missouri. 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. 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.

Education
Linda Randall received the BS at Colorado State University in Zoology and the PhD at University of Wisconsin in Molecular Biology.

Academic Research Career
Linda Randall was a professor at University of Uppsala, Sweden for eight years and joined the faculty at Washington State University in 1981. 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. 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. The two professors took over three quarters of a million dollars in federal research funding with them to Missouri.

Linda Randall showed the mechanism of protein export in the bacterium Escherichia coli. 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. 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. 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. Her development of a system to study membrane translocation in the test tube has been important in her own research and that of others.

Honors and Awards
National Academy of Sciences, 1997

American Academy of Microbiology

American Academy of Arts and Sciences, 1984

Fellow of American Association for the Advancement of Science

Eli Lilly Award in Microbiology or Immunology (American Society for Microbiology)

Selected Works
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