期刊
MOLECULAR CELL
卷 66, 期 4, 页码 558-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2017.04.023
关键词
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资金
- Deutsche Forschungsgemeinschaft [SFB860, FOR1805]
- Boehringer Ingelheim Foundation
Ribosome frameshifting during translation of bacterial dnaX can proceed via different routes, generating a variety of distinct polypeptides. Using kinetic experiments, we show that-1 frameshifting predominantly occurs during translocation of two tRNAs bound to the slippery sequence codons. This pathway depends on a stem-loop mRNA structure downstream of the slippery sequence and operates when aminoacyl-tRNAs are abundant. However, when aminoacyl-tRNAs are in short supply, the ribosome switches to an alternative frameshifting pathway that is independent of a stem-loop. Ribosome stalling at a vacant 0-frame A-site codon results in slippage of the P-site peptidyl-tRNA, allowing for-1-frame decoding. When the-1-frame aminoacyl-tRNA is lacking, the ribosomes switch into-2 frame. Quantitative mass spectrometry shows that the-2-frame product is synthesized in vivo. We suggest that switching between frameshifting routes may enrich gene expression at conditions of aminoacyl-tRNA limitation.
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