Article
Mutations at the accommodation gate of the ribosome impair RF2-dependent translation termination.
RNA (New York, N.Y.) - 1 Sept 2010
Burakovsky Dmitry E, Sergiev Petr V, Steblyanko Maria A, Kubarenko Andriy V, Konevega Andrey L, Bogdanov Alexey A, Rodnina Marina V, Dontsova Olga A
Abstract excerpt
During protein synthesis, aminoacyl-tRNA (aa-tRNA) and release factors 1 and 2 (RF1 and RF2) have to bind at the catalytic center of the ribosome on the 50S subunit where they take part in peptide bond formation or peptidyl-tRNA hydrolysis, respectively. Computer simulations of aa-tRNA movement into the catalytic site (accommodation) suggested that three nucleotides of 23S rRNA, U2492, C2556, and C2573, form a...
Topics
- Escherichia coli
- Escherichia coli Proteins
- Mutagenesis, Site-Directed
- Mutation
- Peptide Chain Termination, Translational
- Peptide Termination Factors
- Protein Biosynthesis
- RNA, Ribosomal, 23S
- RNA, Transfer
- Ribosomes