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チバ シノブ
CHIBA SHINOBU
千葉 志信 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2024/09 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Resolution of ribosomal stalling by EF-P and ABCF ATPases YfmR and YkpA/YbiT. |
| 執筆形態 | 共著 |
| 掲載誌名 | Nucleic acids research |
| 掲載区分 | 国外 |
| 巻・号・頁 | 52(16),pp.9854-9866 |
| 国際共著 | 国際共著 |
| 著者・共著者 | Takada Hiraku, Fujiwara Keigo, Atkinson Gemma C, Chiba Shinobu, Hauryliuk Vasili |
| 概要 | Efficiency of protein synthesis on the ribosome is strongly affected by the amino acid composition of the assembled amino acid chain. Challenging sequences include proline-rich motifs as well as highly positively and negatively charged amino acid stretches. Members of the F subfamily of ABC ATPases (ABCFs) have been long hypothesised to promote translation of such problematic motifs. In this study we have applied genetics and reporter-based assays to characterise the four housekeeping ABCF ATPases of Bacillus subtilis: YdiF, YfmM, YfmR/Uup and YkpA/YbiT. We show that YfmR cooperates with the translation factor EF-P that promotes translation of Pro-rich motifs. Simultaneous loss of both YfmR and EF-P results in a dramatic growth defect. Surprisingly, this growth defect can be largely suppressed though overexpression of an EF-P variant lacking the otherwise crucial 5-amino-pentanolylated residue K32. Using in vivo reporter assays, we show that overexpression of YfmR can alleviate ribosomal stalling on Asp-Pro motifs. Finally, we demonstrate that YkpA/YbiT promotes translation of positively and negatively charged motifs but is inactive in resolving ribosomal stalls on proline-rich stretches. Collectively, our results provide insights into the function of ABCF translation factors in modulating protein synthesis in B. subtilis. |
| DOI | 10.1093/nar/gkae556 |
| ISSN | 1362-4962 |
| PMID | 38943426 |