Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1

被引：577

作者：

Cope, GA

Suh, GSB

Aravind, L

Schwarz, SE

Zipursky, SL

Koonin, EV

Deshaies, RJ ^{[1
]}

机构：

[1] CALTECH, Dept Biol, Pasadena, CA 91125 USA

[2] Univ Calif Los Angeles, Sch Med, Dept Biol Chem, Los Angeles, CA 90095 USA

[3] Natl Lib Med, Natl Ctr Biotechnol Informat, NIH, Bethesda, MD 20894 USA

来源：

SCIENCE | 2002年 / 298卷 / 5593期

关键词：

D O I：

10.1126/science.1075901

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

COP9 signalosome (CSN) cleaves the ubiquitin-like protein Nedd8 from the Cul1 subunit of SCF ubiquitin ligases. The Jab1/MPN domain metalloenzyme (JAMM) motif in the Jab1/Csn5 subunit was found to underlie CSN's Nedd8 isopeptidase activity. JAMM is found in proteins from archaea, bacteria, and eukaryotes, including the Rpn11 subunit of the 26 S proteasome. Metal chelators and point mutations within JAMM abolished CSN-dependent cleavage of Nedd8 from Cul1, yet had little effect on CSN complex assembly. Optimal SCF activity in yeast and both viability and proper photoreceptor cell ( R cell) development in Drosophila melanogaster required an intact Csn5 JAMM domain. We propose that JAMM isopeptidases play important roles in a variety of physiological pathways.

引用

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页码：608 / 611

页数：4

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