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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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| 言語種別 | 英語 |
| 発行・発表の年月 | 1997/05 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion |
| 執筆形態 | その他 |
| 掲載誌名 | JOURNAL OF BIOLOGICAL CHEMISTRY |
| 出版社・発行元 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| 巻・号・頁 | 272(20),pp.12889-12892 |
| 著者・共著者 | S Nishikawa,T Endo |
| 概要 | DnaJ-like proteins are functional partners for Hsp70 molecular chaperones, Complete nucleotide sequencing of yeast chromosome X has revealed that an open reading frame YJL073w encodes a novel member of the DnaJ-like protein family. The open reading frame represents a protein of 692 amino acids with a J-domain and one putative membrane-spanning segment. An epitope-tagged version of the protein was anchored in the endoplasmic reticulum (ER) membrane and its J-domain faced the ER lumen. We therefore propose to designate this gene JEM1 (DnaJ-like protein of the ER membrane) and to designate its gene product JEM1p. The JEM1 gene is not essential for cell growth, but double disruption of the JEM1 gene and the SCJ1 gene, which encodes another DnaJ-like protein in the ER lumen, causes growth arrest at elevated temperature. The Delta jem1 mutant is defective in nuclear fusion, karyogamy, during mating. A mutant JEM1p carrying a mutation in the highly conserved His-Pro-Asp sequence in the J-domain could not complement either temperature-sensitive growth of the Delta jem1 Delta scj1 double mutant or defects in karyogamy of the Delta jem1 mutant. JEM1p likely assists the functions of BiP, Hsp70 in the ER, including karyogamy. |
| ISSN | 0021-9258 |