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Ubiquitin system: JAMMing in the name of the lid
Christoph Berndt1, Dawadschargal Bech-Otschir, Wolfgang Dubiel
1Department of Surgery, Division of Molecular Biology, Monbijoustrasse 2, 10117 Berlin, Germany.
Current Biology : CB
|December 13, 2002
Abstract:
The isopeptide bonds formed by ubiquitin or its relatives are cleaved by hydrolases with active site cysteines. Recent studies have revealed that similar metalloprotease motifs--JAMMs--in the Rpn11 subunit of the 26S proteasome lid and in the Csn5 subunit of the COP9 signalosome are involved in deubiquitination and deneddylation, respectively.