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エンドウ トシヤ
ENDO TOSHIYA
遠藤 斗志也 所属 京都産業大学 生命科学部 先端生命科学科 職種 客員教授 |
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| 発行・発表の年月 | 2019/02 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | CdsA is involved in biosynthesis of glycolipid MPIase essential for membrane protein integration in vivo. |
| 執筆形態 | その他 |
| 掲載誌名 | Scientific reports |
| 巻・号・頁 | 9(1),1372頁 |
| 著者・共著者 | Sawasato K,Sato R,Nishikawa H,Iimura N,Kamemoto Y,Fujikawa K,Yamaguchi T,Kuruma Y,Tamura Y,Endo T,Ueda T,Shimamoto K,Nishiyama KI |
| 概要 | MPIase is a glycolipid that is involved in membrane protein integration. Despite evaluation of its functions in vitro, the lack of information on MPIase biosynthesis hampered verification of its involvement in vivo. In this study, we found that depletion of CdsA, a CDP-diacylglycerol synthase, caused not only a defect in phospholipid biosynthesis but also MPIase depletion with accumulation of the precursors of both membrane protein M13 coat protein and secretory protein OmpA. Yeast Tam41p, a mitochondrial CDP-diacylglycerol synthase, suppressed the defect in phospholipid biosynthesis, but restored neither MPIase biosynthesis, precursor processing, nor cell growth, indicating that MPIase is essential for membrane protein integration and therefore for cell growth. Consistently, we observed a severe defect in protein integration into MPIase-depleted membrane vesicles in vitro. Thus, the function of MPIase as a factor involved in protein integration was proven in vivo as well as in vitro. Moreover, Cds1p, a eukaryotic CdsA homologue, showed a potential for MPIase biosynthesis. From these results, we speculate the presence of a eukaryotic MPIase homologue. |
| DOI | 10.1038/s41598-018-37809-8 |
| ISSN | /2045-2322 |
| PMID | 30718729 |