Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1-Reference-Cited by-同舟云学术

Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1

Published:2002-10-18 Issue:5593 Volume:298 Page:608-611
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Cope Gregory A.¹,Suh Greg S. B.²,Aravind L.³,Schwarz Sylvia E.¹,Zipursky S. Lawrence⁴²,Koonin Eugene V.³,Deshaies Raymond J.¹⁴

Affiliation:

1. Department of Biology, California Institute of Technology (CalTech), Pasadena, CA 91125, USA.

2. Department of Biological Chemistry, The School of Medicine, University of California at Los Angeles (UCLA), Los Angeles, CA 90095, USA.

3. National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.

4. Howard Hughes Medical Institute,

Abstract

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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