ALBERT E. DAHLBERG

Professor
Graduate Program in Molecular and Cell Biology and Biochemistry
M.D., University of Chicago School of Medicine, 1965
Ph.D., University of Chicago, 1968
(401) 863-2223

[email protected]

Research Summary

Understanding the catalytic role of ribosomal RNA in protein synthesis has been the central focus of my laboratory for a number of years. Our primary approach has involved the use of genetic methods, specifically mutagenesis of plasmid-encoded rDNA. We have investigated numerous regions of E. coli 16S and 23S rRNA to decipher both the higher order structure and the dynamic aspects of ribosome function.

More recently we have been developing a similar system in the extreme thermophile Thermus thermophilus. The atomic coordinates provided by crystal studies of the 30S and 50S subunits are used in designing mutagenic strategies to probe tRNA selection, translocation, peptide bond formation and signal transmission within and between the subunits. These same methods are being applied to investigate the mechanism of action and resistance of antibiotics affecting protein synthesis.

Selected Publications

Dahlberg, A.E. (2001) "The Ribosome in Action."Science, 292, 868-869.

Bayfield, M., Dahlberg, A.E., Schulmeister U., Dorner, S. and Barta, A. (2001)
"A Conformational Change in the Ribosomal Peptidyl Transferase Center Upon Active/Inactive Transition." Proc. Natl. Acad. Sci. USA, 98, 10,091-10,101.

Gregory,S., Bayfield, M., O'Connor, M., Thompson, J. & A. Dahlberg (2002) "Probing ribosome structure and function by mutagenesis" in Cold Spring Harbor Symposium on Quantitative Biology, LXVI, The Ribosome, Cold Spring Harbor Laboratory Press, 101-108.

Cameron, D., Thompson, J., March, P. & A.Dahlberg (2002) "Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the E. coli ribosome". J. Mol. Biol. 319, 27-35.


Thompson,J., O'Connor, M., Mills, J. & A. Dahlberg (2002) "The protein synthesis inhibitors oxazolidinones and chloramphenicol cause extensive translational inaccuracy in vivo". J. Mol Biol. 322, 273-279.

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