Summary information and primary citation
- PDB-id
-
4zux;
DSSR-derived features in text and
JSON formats
- Class
- hydrolase-DNA
- Method
- X-ray (3.82 Å)
- Summary
- Saga dub module ubp8-sgf11-sus1-sgf73 bound to
ubiqitinated nucleosome
- Reference
-
Morgan MT, Haj-Yahya M, Ringel AE, Bandi P, Brik A,
Wolberger C (2016): "Structural
basis for histone H2B deubiquitination by the SAGA DUB
module." Science, 351,
725-728. doi: 10.1126/science.aac5681.
- Abstract
- 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 patch. The
Ubp8 catalytic domain mediates additional contacts with
H2B, as well as with the conjugated ubiquitin. We find that
the DUB module deubiquitinates H2B both in the context of
the nucleosome and in H2A/H2B dimers complexed with the
histone chaperone, FACT, suggesting that SAGA could target
H2B at multiple stages of nucleosome disassembly and
reassembly during transcription.
