4ZUX

SAGA DUB module Ubp8/Sgf11/Sus1/Sgf73 bound to ubiqitinated nucleosome

Summary for 4ZUX

• Entry DOI: 10.2210/pdb4zux/pdb
• Descriptor: Histone H3.2, Polyubiquitin-B, SAGA-associated factor 73, ... (12 entities in total)
• Functional Keywords: dub, deubiquitinase, usp, chromatin, eraser, nucleosome, modified histone, macromolecular complex, hydrolase-dna complex, hydrolase/dna
• Biological source: Xenopus laevis (African clawed frog); More
• Cellular location: Nucleus: P84233 P53165 P62799 P06897 P02281 P50102 A6ZWK1; Ubiquitin: Cytoplasm : P0CG47; Nucleus, nucleoplasm: Q6WNK7
• Total number of polymer chains: 40
• Total formula weight: 784450.18

Authors

Morgan, M.,Wolberger, C. (deposition date: 2015-05-17, release date: 2016-02-24, Last modification date: 2024-11-20)

Primary citation

Morgan, M.T.,Haj-Yahya, M.,Ringel, A.E.,Bandi, P.,Brik, A.,Wolberger, C.
Structural basis for histone H2B deubiquitination by the SAGA DUB module.
Science, 351:725-728, 2016

PubMed 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.

PubMed: 26912860
DOI: 10.1126/science.aac5681

Experimental method

X-RAY DIFFRACTION (3.82 Å)