Linda Randall

Professor of Biochemistry

Phone:	(573) 884-4160
Lab:	(573) 884-6334
Fax:	(573) 882-5635
Mailing Address:	Biochemistry 117 Schweitzer Hall University of Missouri-Columbia Columbia, MO 65211
Research Areas:	Molecular chaperones in protein export; analysis of protein-protein interactions.

Educational Background

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. The approaches taken in these studies range from biochemical and biophysical techniques to studies carried out in vivo and in cell-free translocation systems. Some of the biophysical techniques we use are static and dynamic light scatter coupled with high performance liquid chromatography, isothermal titration calorimetry, fluorescence spectroscopy, electron paramagnetic resonance (EPR) spectroscopy and analytical centrifugation.

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.