Structural basis for histone H2B deubiquitination by the SAGA DUB module

Morgan, Michael T.; Haj-Yahya, Mahmood; Ringel, Alison E.; Bandi, Prasanthi; Brik, Ashraf; Wolberger, Cynthia

doi:10.1126/science.aac5681

Title: Structural basis for histone H2B deubiquitination by the SAGA DUB module

Journal Article · Fri Feb 12 00:00:00 EST 2016 · Science

DOI:https://doi.org/10.1126/science.aac5681· OSTI ID:1249222

Morgan, Michael T. ^[1]; Haj-Yahya, Mahmood ^[2]; Ringel, Alison E. ^[1]; Bandi, Prasanthi ^[1]; Brik, Ashraf ^[3]; Wolberger, Cynthia ^[1]

Johns Hopkins Univ., Baltimore, MD (United States). School of Medicine. Dept. of Biophysics and Biophysical Chemistry
Ben-Gurion Univ. of the Negev, Beer Sheva (Israel). Dept. of Chemistry
Technion-Israel Inst. of Technology, Haifa (Israel). Schulich Faculty of Chemistry

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. In this paper, 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. Finally, 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.

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Research Organization:: Johns Hopkins Univ., Baltimore, MD (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Inst. of Health (NIH) (United States)

Contributing Organization:: Ben-Gurion Univ. of the Negev, Beer Sheva (Israel); Technion-Israel Inst. of Technology, Haifa (Israel)

Grant/Contract Number:: AC02-06CH11357; GM-095822; Y1-CO-1020; Y1-GM-1104

OSTI ID:: 1249222

Journal Information:: Science, Vol. 351, Issue 6274; ISSN 0036-8075

Publisher:: AAASCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 177 works

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Journal Article · Fri Aug 31 00:00:00 EDT 2012 · Structure · OSTI ID:1249222

Samara, Nadine L; Ringel, Alison E; Wolberger, Cynthia

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59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES

Title: Structural basis for histone H2B deubiquitination by the SAGA DUB module

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