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. 2002 Oct 18;298(5593):608-11.
doi: 10.1126/science.1075901. Epub 2002 Aug 15.

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

Gregory A Cope  1 , Greg S B Suh, L Aravind, Sylvia E Schwarz, S Lawrence Zipursky, Eugene V Koonin, Raymond J Deshaies
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Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1

Gregory A Cope et al. Science. .
Free article

Abstract (V体育2025版)

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 VSports手机版. 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. .

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