| Literature DB >> 28483649 |
Pengse Po1, Erin Delaney1, Howard Gamper2, D Miklos Szantai-Kis3, Lee Speight4, LiWei Tu1, Andrey Kosolapov1, E James Petersson4, Ya-Ming Hou2, Carol Deutsch5.
Abstract
All proteins are synthesized by the ribosome, a macromolecular complex that accomplishes the life-sustaining tasks of faithfully decoding mRNA and catalyzing peptide bond formation at the peptidyl transferase center (PTC). The ribosome has evolved an exit tunnel to host the elongating new peptide, protect it from proteolytic digestion, and guide its emergence. It is here that the nascent chain begins to fold. This folding process depends on the rate of translation at the PTC. We report here that besides PTC events, translation kinetics depend on steric constraints on nascent peptide side chains and that confined movements of cramped side chains within and through the tunnel fine-tune elongation rates.Entities:
Keywords: nascent peptide elongation; ribosome; side-chain dependent elongation rates; translation; unnatural amino acid incorporation
Mesh:
Substances:
Year: 2017 PMID: 28483649 PMCID: PMC5511029 DOI: 10.1016/j.jmb.2017.04.019
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469