title: Ubiquitin system: JAMMing in the name of the lid.
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.
authors.affiliation: Department of Surgery, Division of Molecular Biology, Monbijoustrasse 2, 10117 Berlin, Germany.
authors.forename: Christoph
authors.initials: C
authors.lastname: Berndt
authors.forename: Dawadschargal
authors.initials: D
authors.lastname: Bech-Otschir
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Dubiel
authors.forename: Michael
authors.initials: M
authors.lastname: Seeger
mesh_terms: D008666:Metalloendopeptidases / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D021122:Protein Subunits; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D015398:Signal Transduction; D025801:Ubiquitin / Q000378:metabolism*
chemical_list: D021122:Protein Subunits; D025801:Ubiquitin; D010447:Peptide Hydrolases; D008666:Metalloendopeptidases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease