Ontology highlight
ABSTRACT:
SUBMITTER: Morgan MT
PROVIDER: S-EPMC4863942 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Morgan Michael T MT Haj-Yahya Mahmood M Ringel Alison E AE Bandi Prasanthi P Brik Ashraf A Wolberger Cynthia C
Science (New York, N.Y.) 20160201 6274
Monoubiquitinated histone H2B plays multiple roles in transcription activation. H2B is deubiquitinated by the Spt-Ada-Gcn5 acetyltransferase (SAGA) coactivator, which contains a four-protein subcomplex known as the deubiquitinating (DUB) module. The crystal structure of the Ubp8/Sgf11/Sus1/Sgf73 DUB module bound to a ubiquitinated nucleosome reveals that the DUB module primarily contacts H2A/H2B, with an arginine cluster on the Sgf11 zinc finger domain docking on the conserved H2A/H2B acidic pat ...[more]