Linda Randall
Wurdack Professor of Biological Chemistry
Professor of Biochemistry
Member, National Academy of Sciences
Office: 203A Stephens Hall
Mail: Biochemistry
117 Schweitzer Hall
University of Missouri
Columbia, MO 65211
Phone: 573-884-4160
Fax: 573-882-5635
Lab: 573-884-6334
Educational background
| Degree | School | Location | Major |
| BS | Colorado State University | Fort Collins, Colo. | Zoology |
| PhD | University of Wisconsin | Madison, Wis. | Molecular Biology |
Notable honors and service
- Member, National Academy of Sciences
- Member, American Academy of Arts and Sciences
- Fellow, American Academy of Microbiology
- Fellow, American Association for the Advancement of Science
- Eli Lilly Award in Microbiology or Immunology, 1984
- Executive Council: Protein Society (1996-99)
- MERIT Award NIH (1993-03)
- Conference Organization
- Chair Gordon Conference on Bacterial Cell Surface, 1988
- Co-organizer 14th Symposium of the Protein Society, 2000
- Editorial Boards
- Journal of Bacteriology (1982-1997)
- Protein Science (1992-1996)
Research description
We aim to elucidate the mechanism of protein export in Escherichia coli with emphasis on the interactions of the protein components of the pathway. Translocation of specific, newly synthesized polypeptides across biological membranes is a ubiquitous process that is essential for living cells. Whether the process occurs in eukaryotes or in prokaryotes in almost all cases molecular chaperones are involved. Chaperones are a family of proteins that display the remarkable ability to recognize and bind polypeptides based on the fact that the ligands are in a nonnative state.
Our research is focused on the molecular chaperone SecB and its promiscuous interactions with polypeptide ligands as well as its specific interactions with the protein SecA, which is an ATPase that serves as the motor for transfer of proteins across the membrane. We study the interactions among the proteins using a wide range of techniques. These include the following biophysical techniques: column chromatography, dynamic light scattering, calorimetry, fluorescence spectroscopy, analytical centrifugation, mass spectrometry, and electron paramagnetic spin resonance. We also have established an in vitro protein translocation system and assays of the ATPase activity of SecA.
Selected publications
Woodbury, R.L., Hardy, S.J.S. and Randall, L.L. 2002. Complex behavior in solution of homodimeric SecA. Protein Science 11:875-882.
Randall, L.L. and Hardy, S.J.S. 2002. SecB, one small chaperone in the complex milieu of the cell. Cellular and Molecular Life Sciences. 59:1617-1623.
Randall, L.L., Crane, J.M., Liu, G. and Hardy, S.J.S. 2004. Sites of Interaction between SecA and the Chaperone SecB, Two Proteins involved in Export. Protein Science. 13:1124-1133.
Randall L.L., Crane J.M., Lilly A.A., Liu G., Mao C., Patel C.N., Hardy S.J. 2005. Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export. J Mol Biol. 348(2):479-89.
Patel, C. N., Smith, V. F., and Randall, L. L. 2006. Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export. Protein Science. 15: 1379-1386.
Crane, J. M., Suo, Y., Lilly, A. A., Mao, C. Hubbell, W. L., and Randall, L. L. 2006. Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling. J. Mol. Biol. 363: 63-74.
Cooper D.B., Smith V.F., Crane J.M., Roth H.C., Lilly A.A., Randall L.L. (2008) SecA, the motor of the secretion machine, binds diverse partners on one interactive surface. J. Mol. Biol. 382: 74-87
Mao C., Hardy S.J., Randall L.L. (2009) Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA. J. Bacteriol. 191: 978-84
Lilly A.A., Crane J.M., Randall L.L. (2009) Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands. Protein Sci. 18: 1860-1868