Unknown

Dataset Information

0

Contribution of ribosomal residues to P-site tRNA binding.


ABSTRACT: Structural studies have revealed multiple contacts between the ribosomal P site and tRNA, but how these contacts contribute to P-tRNA binding remains unclear. In this study, the effects of ribosomal mutations on the dissociation rate (k(off)) of various tRNAs from the P site were measured. Mutation of the 30S P site destabilized tRNAs to various degrees, depending on the mutation and the species of tRNA. These data support the idea that ribosome-tRNA interactions are idiosyncratically tuned to ensure stable binding of all tRNA species. Unlike deacylated elongator tRNAs, N-acetyl-aminoacyl-tRNAs and tRNA(fMet) dissociated from the P site at a similar low rate, even in the presence of various P-site mutations. These data provide evidence for a stability threshold for P-tRNA binding and suggest that ribosome-tRNA(fMet) interactions are uniquely tuned for tight binding. The effects of 16S rRNA mutation G1338U were suppressed by 50S E-site mutation C2394A, suggesting that G1338 is particularly important for stabilizing tRNA in the P/E site. Finally, mutation C2394A or the presence of an N-acetyl-aminoacyl group slowed the association rate (k(on)) of tRNA dramatically, suggesting that deacylated tRNA binds the P site of the ribosome via the E site.

SUBMITTER: Shoji S 

PROVIDER: S-EPMC2709574 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Contribution of ribosomal residues to P-site tRNA binding.

Shoji Shinichiro S   Abdi Nimo M NM   Bundschuh Ralf R   Fredrick Kurt K  

Nucleic acids research 20090505 12


Structural studies have revealed multiple contacts between the ribosomal P site and tRNA, but how these contacts contribute to P-tRNA binding remains unclear. In this study, the effects of ribosomal mutations on the dissociation rate (k(off)) of various tRNAs from the P site were measured. Mutation of the 30S P site destabilized tRNAs to various degrees, depending on the mutation and the species of tRNA. These data support the idea that ribosome-tRNA interactions are idiosyncratically tuned to e  ...[more]

Similar Datasets

| S-EPMC3001080 | biostudies-literature
| S-EPMC4143144 | biostudies-literature
| S-EPMC3017606 | biostudies-literature
| S-EPMC1220128 | biostudies-other
| S-EPMC2453706 | biostudies-literature
| S-EPMC6822507 | biostudies-literature
| S-EPMC4150856 | biostudies-literature
| S-EPMC3234781 | biostudies-literature
| S-EPMC2752669 | biostudies-literature
| S-EPMC2873144 | biostudies-literature