Abstract
Nascent peptide-dependent translation arrest is crucial for the quality control of eukaryotic gene expression. Here we show that the receptor for activated C kinase 1 (RACK1) participates in nascent peptide-dependent translation arrest, and that its binding to the 40S subunit is crucial for this. Translation arrest by a nascent peptide results in Dom34/Hbs1-independent endonucleolytic cleavage of mRNA, and this is stimulated by RACK1. We propose that RACK1 stimulates the translation arrest that is induced by basic amino-acid sequences that leads to endonucleolytic cleavage of the mRNA, as well as to co-translational protein degradation.
Original language | English |
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Pages (from-to) | 956-961 |
Number of pages | 6 |
Journal | EMBO Reports |
Volume | 11 |
Issue number | 12 |
DOIs | |
Publication status | Published - 2010 Dec |
Externally published | Yes |
Keywords
- RACK1
- endonucleolytic cleavage
- mRNA quality control
- nascent peptide
- translation arrest
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Genetics