Welcome to Gaia! :: View User's Journal | Gaia Journals

Acknowledgments
We thank Tadayuki Imanaka and Haruyuki Atomi for the use of their DNA sequencer. This work was supported in part by a Grant-in-Aid for Scientific Research on Priority Areas from the Ministry of Education, Culture, Sports, Science and Technology of Japan to T.S.
Keywords
Ubiquitin; De-ubiquitinating enzyme; Proteasome; X-ray crystallography
Introduction
The de-ubiquitinating enzymes (DUBs) are ubiquitin-specific proteases that can disassemble the ubiquitin from an adduct target molecule. This process is implicated in important cellular processes including CKI 2A control, DNA repair, oncoprotein degradation, maintenance of chromatin structure, endocytosis, kinase signaling pathways, antigen presentation, and the degradation of abnormal proteins. The DUBs family consists of five distinct sub-families. Four sub-families are papain-like cysteine proteases: the ubiquitin C-terminal hydrolases (UCHs), the ubiquitin-specific proteases (USPs/UBPs), the ovarian tumor (OUT) domain, and the Josephin domain (MJD) DUBs. The fifth family is a collection of zinc-dependent metalloproteases, for example the JAB1.MPN/Mov34 metalloenzyme (JAMM) domain protease [9] and [10].