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James Bodley

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Title

James Bodley
Emeritus faculty

Department:

BMBB Tenure: 1967-1988

Research Interests:
Protein biosynthesis and RNA structure and function.

Classic Papers

Bodley, J.W., Zieve, J.F. and Lin, L., "Studies on Translocation IV: The Hydrolysis of a Single Round of GTP in the Presence of Fusidic Acid", J. Biol. Chem. 245, 5662 (1970).

Elongation factor G plays a central role in protein synthesis by moving the ribosome along mRNA following each amino acid addition to growing proteins. This work defined the novel mechanism by which fusidic acid inhibits this reaction by preventing the dissociation of EFG and GDP from the ribosome. The resulting Ribosome-EFG-GDP complex has become a major landmark in mapping the functional topology of the ribosome.

Van Ness, B.G., Howard, J.B. and Bodley, J.W., "ADP?Ribosylation of Elongation Factor 2 by Diphtheria Toxin: NMR Spectra and Proposed Structures of Ribosyl?Diphthamide and its Hydrolysis Products", J. Biol. Chem. 255, 10710 (1980).

This work identified the unique chemical structure in EF2 that is responsible for its recognition and inactivation by diphtheria toxin as the essential step in diphtheria intoxication. Diphthamide is now recognized as one of the most complex and specific examples of the posttranslational modification reactions that expand the amino acid repertoire of proteins.

Bailey, S., Wichitwechkarn, J., Johnson, D., Reilly, B.E., Anderson, D.L. and Bodley, J.W., "Phylogenetic Analysis and Secondary Structure of the Bacillus subtilis Bacteriophage RNA Required for DNA Packaging", J. Biol. Chem. 265, 22365 (1990).

This work defined the structure of a unique RNA molecule that plays an essential role in the packaging of DNA, thus setting the stage to understand the mechano-chemical nature of the reaction and a new biological role of RNA.

Email Address

Address
D608 Mayo
420 Delaware St. SE
Minneapolis, MN 55455