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Another look at mutations in ribosomal protein S4 lends strong support to the domain closure model.

Authors
  • Fredrick, Kurt
Type
Published Article
Journal
Journal of Bacteriology
Publisher
American Society for Microbiology
Publication Date
Mar 01, 2015
Volume
197
Issue
6
Pages
1014–1016
Identifiers
DOI: 10.1128/JB.02579-14
PMID: 25548248
Source
Medline
License
Unknown

Abstract

Ribosomes employ a "kinetic discrimination" mechanism, in which correct substrates are incorporated more rapidly than incorrect ones. The structural basis of this mechanism may involve 30S domain closure, a global conformational change that coincides with codon recognition. In a direct screen for fidelity-altering mutations, Agarwal and coworkers (D. Agarwal, D. Kamath, S. T. Gregory, and M. O'Connor, J Bacteriol 197:1017-1025, 2015, doi:10.1128/JB.02485-14) isolated mutations that progressively truncate the C terminus of S4. All of these promote miscoding and undoubtedly destabilize the S4-S5 interface, consistent with the domain closure model.

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