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

Science  18 Oct 2002:
Vol. 298, Issue 5593, pp. 608-611
DOI: 10.1126/science.1075901

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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 26S 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.

  • * Present address: Department of Biology, California Institute of Technology, Pasadena, CA 91125, USA.

  • Present address: G2M Cancer Drugs AG, Frankfurt/Main, Germany.

  • To whom correspondence should be addressed. E-mail: deshaies{at}caltech.edu

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