Class of 2006
memcdonald@jhu.edu | B.S. Biophysics, Davidson College
Research
Protein translation is one of the most important events in a cell. While there are many aspects of translation that can be studied such as initiation, elongation, and regulation, I am focused on the termination of protein synthesis. Translation termination is signaled in all organisms by one of three nearly universal stop codons in the ribosomal A site. These stop codons are decoded by a protein known as Release Factor (RF), instead of the tRNAs that decode all other sense codons. When a class I RF recognizes a stop codon, it catalyzes the hydrolysis that releases the completed protein chain from the P-site tRNA on the ribosome. Translation termination has not been as well studied as several other aspects of translation, and a clear understanding of the exact mechanism has yet to be determined. My project attempts to get a better understanding of translation termination using both bulk approaches and single molecule FRET to follow RF1 as it interacts with the ribosome and its components, and releases a polypeptide. We are interested in the kinetics of the reaction, the structure of RF as it catalyzes release, and how this reaction is affected by the addition of other components such as the class II RF (RF3), and drugs such as aminoglycosides.
Publications
Youngman, E.M., M.E. McDonald, and R. Green. (2008) Peptide Release on the Ribosome: Mechanism and Implications for Translational Control. Annu. Rev. Microbiol. (in press)
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