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Maintenance of the correct open reading frame by the ribosome
Author(s) -
Hansen Thomas M,
Baranov Pavel V,
Ivanov Ivaylo P,
Gesteland Raymond F,
Atkins John F
Publication year - 2003
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.embor825
Subject(s) - transfer rna , open reading frame , translational frameshift , genetics , a site , ribosome , biology , ribosome profiling , protein biosynthesis , translation (biology) , computational biology , p site , rna , messenger rna , binding site , gene , peptide sequence
During translation, a string of non‐overlapping triplet codons in messenger RNA is decoded into protein. The ability of a ribosome to decode mRNA without shifting between reading frames is a strict requirement for accurate protein biosynthesis. Despite enormous progress in understanding the mechanism of transfer RNA selection, the mechanism by which the correct reading frame is maintained remains unclear. In this report, evidence is presented that supports the idea that the translational frame is controlled mainly by the stability of codon–anticodon interactions at the P site. The relative instability of such interactions may lead to dissociation of the P‐site tRNA from its codon, and formation of a complex with an overlapping codon, the process known as P‐site tRNA slippage. We propose that this process is central to all known cases of +1 ribosomal frameshifting, including that required for the decoding of the yeast transposable element Ty 3 . An earlier model for the decoding of this element proposed ‘out‐of‐frame’ binding of A‐site tRNA without preceding P‐site tRNA slippage.