Journal
MOLECULAR CELL
Volume 41, Issue 3, Pages 321-330Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2010.12.031
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Funding
- National Science Foundation [MCB-0824739]
- Chicago Biomedical Consortium
- Chicago Community Trust
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0824739] Funding Source: National Science Foundation
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The ability to monitor the nascent peptide structure and to respond functionally to specific nascent peptide sequences is a fundamental property of the ribosome. An extreme manifestation of such response is nascent peptide-dependent ribosome stalling, involved in the regulation of gene expression. The molecular mechanisms of programmed translation arrest are unclear. By analyzing ribosome stalling at the regulatory cistron of the antibiotic resistance gene ermA, we uncovered a carefully orchestrated cooperation between the ribosomal exit tunnel and the A-site of the peptidyl transferase center (PTC) in halting translation. The presence of an inducing antibiotic and a specific nascent peptide in the exit tunnel abrogate the ability of the PTC to catalyze peptide bond formation with a particular subset of amino acids. The extent of the conferred A-site selectivity is modulated by the C-terminal segment of the nascent peptide, where the third-from-last residue plays a critical role.
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