Ontology highlight
ABSTRACT:
SUBMITTER: Schrader JM
PROVIDER: S-EPMC3069205 | biostudies-literature | 2011 Mar
REPOSITORIES: biostudies-literature
Schrader Jared M JM Chapman Stephen J SJ Uhlenbeck Olke C OC
Proceedings of the National Academy of Sciences of the United States of America 20110314 13
To better understand why aminoacyl-tRNAs (aa-tRNAs) have evolved to bind bacterial elongation factor Tu (EF-Tu) with uniform affinities, mutant tRNAs with differing affinities for EF-Tu were assayed for decoding on Escherichia coli ribosomes. At saturating EF-Tu concentrations, weaker-binding aa-tRNAs decode their cognate codons similarly to wild-type tRNAs. However, tighter-binding aa-tRNAs show reduced rates of peptide bond formation due to slow release from EF-Tu•GDP. Thus, the affinities of ...[more]