Unknown

Dataset Information

0

Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding.


ABSTRACT: 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 aa-tRNAs for EF-Tu are constrained to be uniform by their need to bind tightly enough to form the ternary complex but weakly enough to release from EF-Tu during decoding. Consistent with available crystal structures, the identity of the esterified amino acid and three base pairs in the T stem of tRNA combine to define the affinity of each aa-tRNA for EF-Tu, both off and on the ribosome.

SUBMITTER: Schrader JM 

PROVIDER: S-EPMC3069205 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Tuning the affinity of aminoacyl-tRNA to elongation factor Tu for optimal decoding.

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]

Similar Datasets

| S-EPMC4159200 | biostudies-literature
| S-EPMC8259901 | biostudies-literature
| S-EPMC7035488 | biostudies-literature
| S-EPMC3232051 | biostudies-literature
| S-EPMC4880308 | biostudies-literature
| S-EPMC8565323 | biostudies-literature
| S-EPMC2666022 | biostudies-literature
| S-EPMC4156062 | biostudies-literature
| S-EPMC6144866 | biostudies-literature
| S-EPMC2648704 | biostudies-literature