期刊
EUKARYOTIC CELL
卷 14, 期 1, 页码 86-95出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/EC.00106-14
关键词
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资金
- European Research Council (ERC)
- Novo Nordisk Foundation Center for Protein Research
- Boehringer Ingelheim Fonds
- Chemischen Industrie
- Deutsche Jose Carreras-Stiftung e.V.
- [Sonderforschungsbereich SFB646]
- [Sonderforschungsbereich SFB684]
Translation is a fundamental and highly regulated cellular process. Previously, we reported that the kinase and transcription elongation factor Ctk1 increases fidelity during translation elongation in Saccharomyces cerevisiae. Here, we show that loss of Ctk1 function also affects the initiation step of translation. Translation active extracts from Ctk1-depleted cells show impaired translation activity of capped mRNA, but not mRNA reporters containing the cricket paralysis virus (CrPV) internal ribosome entry site (IRES). Furthermore, the formation of 80S initiation complexes is decreased, which is probably due to reduced subunit joining. In addition, we determined the changes in the phosphorylation pattern of a ribosome enriched fraction after depletion of Ctk1. Thus, we provide a catalogue of phosphoproteomic changes dependent on Ctk1. Taken together, our data suggest a stimulatory function of Ctk1 in 80S formation during translation initiation.
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