Zinc-finger UBPs: regulators of deubiquitylation.
Deubiquitylating enzymes have key regulatory roles in multiple cellular processes by mediating ubiquitin removal and processing. The ubiquitin-specific processing proteases (USPs) represent the largest subclass of deubiquitylases. Recently, several USPs that recognize the monoubiquitylated histones H2A and/or H2B have been identified. Among these enzymes, three USPs contain a zinc-finger ubiquitin-specific protease (ZnF-UBP) domain, indicating that this domain plays a crucial part in regulating their activity. To address the putative function of this domain, we systematically analysed and aligned yeast and human ZnF-UBP-containing proteins. By complementing our analysis with structural and functional data, we present a classification of the different ZnF-UBP-containing proteins and a model for their regulation.
Bonnet
Jacques
J
Department of Functional Genomics, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS UMR 7104, INSERM U 596, Université Louis Pasteur de Strasbourg, ILLKIRCH Cedex, CU de Strasbourg, France.
Romier
Christophe
C
Tora
László
L
Devys
Didier
D
D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D025801:Ubiquitin / Q000378:metabolism*; D016335:Zinc Fingers
D025801:Ubiquitin; D010450:Endopeptidases; C059237:ubiquitin-Nalpha-protein hydrolase