ID | 46920 |
フルテキストURL | |
著者 |
Sekiguchi, Takeshi
Department of Molecular Biology, Graduate School of Medical Sciences, Kyushu University
Sasaki, Toru
Center for Faculty Development, Okayama University
Funakoshi, Minoru
Center for Faculty Development, Okayama University
Ishii, Takashi
Department of Molecular Biology, Graduate School of Medical Sciences, Kyushu University
Saitoh, Yoh-hei
Department of Molecular Biology, Graduate School of Medical Sciences, Kyushu University
Kaneko, Shu-ichi
Department of Molecular Biology, Graduate School of Medical Sciences, Kyushu University
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抄録 | Ubiquitin-like (UBL)-ubiquitin-associated (UBA) proteins, including Dsk2 and Rad23, act as delivery factors that target polyubiquitinated substrates to the proteasome. We report here that the Dsk2 UBL domain is ubiquitinated in yeast cells and that Dsk2 ubiquitination of the UBL domain is involved in Dsk2 stability, depending on the Dsk2 UBA domain. Also, Dsk2 lacking ubiquitin chains impaired ubiquitin-dependent protein degradation and decreased the interaction of Dsk2 with polyubiquitinated proteins in cells. Moreover, Dsk2 ubiquitination affected ability to restore the temperature-sensitive growth defect of dsk2 Delta. These results indicate that ubiquitination in the UBL domain of Dsk2 has in vivo functions in the ubiquitin-proteasome pathway in yeast.
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キーワード | UBL–UBA protein
Dsk2
UBL domain
UBA domain
Ubiquitin
Proteasome
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発行日 | 2011-08-05
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出版物タイトル |
Biochemical and Biophysical Research Communications
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巻 | 411巻
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号 | 3号
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出版者 | Academic Press Inc Elsevier Science
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開始ページ | 555
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終了ページ | 561
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ISSN | 0006-291X
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NCID | AA00564395
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資料タイプ |
学術雑誌論文
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言語 |
英語
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著作権者 | © 2011 Elsevier Inc. All rights reserved.
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論文のバージョン | author
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査読 |
有り
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DOI | |
PubMed ID | |
Web of Science KeyUT |