Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 411, Issue 2, Pages 499-510Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2011.05.038
Keywords
cysteine accessibility; ribosome-nascent peptide interactions; translation; allosteric rearrangements; solvent-accessible volumes
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Funding
- National Institutes of Health [GM 52302, DC007669]
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Although we have numerous structures of ribosomes, none disclose side-chain rearrangements of the nascent peptide during chain elongation. This study reports for the first time that rearrangement of the peptide and/or tunnel occurs in distinct regions of the tunnel and is directed by the unique primary sequence of each nascent peptide. In the tunnel mid-region, the accessibility of an introduced cysteine to a series of novel hydrophilic maleimide reagents increases with increasing volume of the adjacent chain residue, a sensitivity not manifest at the constriction and exit port. This surprising result reveals molecular movements not yet resolvable from structural studies. These findings map solvent-accessible volumes along the tunnel and provide novel insights critical to our understanding of allosteric communication within the ribosomal tunnel, translational arrest, chaperone interaction, folding, and rates of elongation. (C) 2011 Elsevier Ltd. All rights reserved.
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