David Peabody, Ph.D.

Molecular Genetics and Microbiology
MSC08 4660
1 University of New Mexico
Albuquerque, NM 87131-0001
 
Office: CRTC 316
Tel: (505) 272-0071
Fax: (505) 272-6029
E-mail: dpeabody@unm.edu

Keywords: RNA-protein interactions, translational regulation, virus assembly.

Research Interests

Protein-RNA Interactions. The coat proteins of the RNA bacteriophages of E. coli interact with a stem-loop structure in viral RNA to repress replicase translation and to encapsidate the viral genome. Different RNA phage coat proteins possess similar tertiary structures but bind different RNA structures, providing a convenient model for understanding the basis of specificity in protein-RNA recognition. Making extensive use of genetics and biochemistry, we have characterized the RNA-binding sites of several coat proteins and have learned how to interchange their RNA-binding specificities. These studies are being extended to include investigation of coat protein folding and virus assembly.

For information about post-doc positions in the Peabody lab, see Job Opportunities.

Selected Publications

Lim, F., Downey, T., Peabody D.S. (2001) Specific RNA Binding and Translational Repression by PP7 Coat Protein. J. Biol. Chem. 276: 22507

Powell, A.J., Peabody, D.S. (2001) Asymmetric interactions in the adenosine-binding pockets of the MS2 coat protein dimer. BMC Molecular Biology 2: 6Peabody, D.S. and Chakerian, A. 1999.

Asymmetric Contributions to RNA Binding by the Thr45 Residues of the MS2 Coat Protein Dimer. J. Biol. Chem. 274: 25403-25410.

Convery, M.A., Rowsell, S., Stonehouse, N.J., Ellington, A.D., Hirao, I., Murray, J.B., Peabody, D.S., Phillips, S.E.V., and Stockley, P.G. 1998. Crystal structure of an RNA-aptamer-protein complex at 2.8 angstrom resolution. Nature Structural Biology 5: 133-139.

Rowsell, S., Stonehouse, M.J., Convery, M.A., Adams, C.J., Ellington, A.D., Hirao, I., Peabody, D.S., Stockley, P.G., and Phillips, S.E.V. 1998. Crystal structures of a series of RNA aptamers complexed to the same protein target. Nature Structural Biology 5: 970-975

Spingola, M. and Peabody, D.S. 1997. MS2 coat protein mutants which bind Q-beta RNA. Nucleic Acids Res. 25: 2808-2815.

Peabody, D.S. 1997. Role of the coat protein-RNA interaction in the life cycle of the bacteriophage MS2. Mol. Gen. Genet. 254: 358-364.

Lim, F., Spingola, M., and Peabody, D.S. 1996. The RNA-binding site of Q-beta coat protein. J. Biol. Chem. 271: 31839-31845.

Peabody, D.S. and Lim, F. 1996. Complementation of RNA Binding Site Mutations in Heterodimers of Bacteriophage MS2 Coat Protein. Nucleic Acids Res. 24:2352-2359.

Ni,C.-Z., Syed, R., Kodandapani, R., Wickersham, J., Peabody, D.S., Ely, K.R. 1995. Crystal Structure of th Bacteriophage MS2 Coat Protein Dimer: Implications for Virus Assembly and RNA Binding. Structure 3:255-263.

Lim, F. and Peabody, D.S. 1994. Mutations that Increase the Affinity of a Transitional Repressor for RNA. Nucleic Acids Res. 22:3748-3752.

Lim, F., Spingola, M. and Peabody, D.S. 1994. Altering the RNA Binding Specificity of a Translational Repressor. J. Biol. Chem. 269:9006-9010.

Peabody, D.S. 1993. The RNA-Binding Site of Bacteriophage MS2 Coat Protein. EMBO J. 12:595-600.

Peabody, D.S. and Ely, K.R. 1992. Control of Translational Repression by Protein-Protein Interactions. Nucleic Acids Res. 20:1649-1655.