BBRC441_3_555-561.pdf 587 KB
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
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.
Biochemical and Biophysical Research Communications
Academic Press Inc Elsevier Science
© 2011 Elsevier Inc. All rights reserved.
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