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ミシマ ユウイチロウ
Mishima Yuichiro
三嶋 雄一郎 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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| 発行・発表の年月 | 2023/09 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Znf598-mediated Rps10/eS10 ubiquitination contributes to the ribosome ubiquitination dynamics during zebrafish development |
| 執筆形態 | その他 |
| 掲載誌名 | RNA |
| 出版社・発行元 | Cold Spring Harbor Laboratory |
| 巻・号・頁 | rna.079633.123-rna.079633.123頁 |
| 担当区分 | 最終著者,責任著者 |
| 著者・共著者 | Nozomi Ugajin,Koshi Imami,Hiraku Takada,Yasushi Ishihama,Shinobu Chiba,Yuichiro Mishima |
| 概要 | Ribosome is a translational apparatus that comprises about 80 ribosomal proteins and four rRNAs. Recent studies reported that ribosome ubiquitination is crucial for translational regulation and ribosome-associated quality control (RQC). However, little is known about the dynamics of ribosome ubiquitination under complex biological processes of multicellular organisms. To explore ribosome ubiquitination during animal development, we generated a zebrafish strain that expresses a FLAG-tagged ribosomal protein Rpl36/eL36 from its endogenous locus. We examined ribosome ubiquitination during zebrafish development by combining affinity purification of ribosomes from rpl36-FLAG zebrafish embryos with immunoblotting analysis. Our findings showed that ubiquitination of ribosomal proteins dynamically changed as development proceeded. We also showed that during zebrafish development, the ribosome was ubiquitinated by Znf598, an E3 ubiquitin ligase that activates RQC. Ribosomal protein Rps10/eS10 was found to be a key ubiquitinated protein during development. Furthermore, we showed that Rps10/eS10 ubiquitination-site mutations reduced the overall ubiquitination pattern of ribosome. These results demonstrate the complexity and dynamics of ribosome ubiquitination during zebrafish development. |
| DOI | 10.1261/rna.079633.123 |
| ISSN | 1355-8382/1469-9001 |
| PermalinkURL | https://syndication.highwire.org/content/doi/10.1261/rna.079633.123 |