2020年5月1日
In vitro yeast reconstituted translation system reveals function of eIF5A for synthesis of long polypeptide.
Journal of biochemistry
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- 巻
- 167
- 号
- 5
- 開始ページ
- 451
- 終了ページ
- 462
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1093/jb/mvaa022
We have recently developed an in vitro yeast reconstituted translation system, which is capable of synthesizing long polypeptides. Utilizing the system, we examined the role of eIF5A and its hypusine modification in translating polyproline sequence within long open reading frames. We found that polyproline motif inserted at the internal position of the protein arrests translation exclusively at low Mg2+ concentrations, and peptidylpolyproline-tRNA intrinsically destabilizes 80S ribosomes. We demonstrate that unmodified eIF5A essentially resolves such ribosome stalling; however, the hypusine modification drastically stimulates ability of eIF5A to rescue polyproline-mediated ribosome stalling and is particularly important for the efficient translation of the N-terminal or long internal polyproline motifs.
- ID情報
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- DOI : 10.1093/jb/mvaa022
- PubMed ID : 32053170