We're JAMMing

Science's STKE  22 Oct 2002:
Vol. 2002, Issue 155, pp. tw384-TW384
DOI: 10.1126/stke.2002.155.tw384

A protein motif termed JAMM has been identified that appears to be responsible for encoding a metallo-isopeptidase activity important in cleaving either ubiquitin or ubiquitin-like Nedd8 moieties from proteins (see the Perspective by Hochstrasser). Cope et al. show that in the COP9 signalosome, the JAMM motif acts to de-Neddylate substrates, such as those that are important in eye development. Verma et al. show that in the proteasome lid subcomplex, the JAMM motif is important in cleaving ubiquitin from a variety of substrates, and that inactivation of the JAMM motif is lethal in yeast.

M. Hochstrasser, New proteases in a ubiquitin stew. Science 298, 549-552 (2002). [Summary] [Full Text]

G. A. Cope, G. S. B. Suh, L. Aravind, S. E. Schwarz, S. L. Zipursky, E. V. Koonin, R. J. Deshaies, Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1. Science 298, 608-611 (2002). [Abstract] [Full Text]

R. Verma, L. Aravind, R. Oania, W. H. McDonald, J. R. Yates, III, E. V. Koonin, R. J. Deshaies, Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611-615 (2002). [Abstract] [Full Text]