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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
Kobayashi, Hideki Center for Faculty Development, Okayama University
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.
キーワード
UBL–UBA protein
Dsk2
UBL domain
UBA domain
Ubiquitin
Proteasome
発行日
2011-08-05
出版物タイトル
Biochemical and Biophysical Research Communications
411巻
3号
出版者
Academic Press Inc Elsevier Science
開始ページ
555
終了ページ
561
ISSN
0006-291X
NCID
AA00564395
資料タイプ
学術雑誌論文
言語
English
OAI-PMH Set
岡山大学
著作権者
© 2011 Elsevier Inc. All rights reserved.
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