Structural basis for histone H2B deubiquitination by the SAGA DUB module
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. 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.
- Authors:
-
- 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
- Publication Date:
- Research Org.:
- Johns Hopkins Univ., Baltimore, MD (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); National Inst. of Health (NIH) (United States)
- Contributing Org.:
- Ben-Gurion Univ. of the Negev, Beer Sheva (Israel); Technion-Israel Inst. of Technology, Haifa (Israel)
- OSTI Identifier:
- 1249222
- Grant/Contract Number:
- AC02-06CH11357; GM-095822; Y1-CO-1020; Y1-GM-1104
- Resource Type:
- Journal Article: Accepted Manuscript
- Journal Name:
- Science
- Additional Journal Information:
- Journal Volume: 351; Journal Issue: 6274; Journal ID: ISSN 0036-8075
- Publisher:
- AAAS
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES
Citation Formats
Morgan, Michael T., Haj-Yahya, Mahmood, Ringel, Alison E., Bandi, Prasanthi, Brik, Ashraf, and Wolberger, Cynthia. Structural basis for histone H2B deubiquitination by the SAGA DUB module. United States: N. p., 2016.
Web. doi:10.1126/science.aac5681.
Morgan, Michael T., Haj-Yahya, Mahmood, Ringel, Alison E., Bandi, Prasanthi, Brik, Ashraf, & Wolberger, Cynthia. Structural basis for histone H2B deubiquitination by the SAGA DUB module. United States. https://doi.org/10.1126/science.aac5681
Morgan, Michael T., Haj-Yahya, Mahmood, Ringel, Alison E., Bandi, Prasanthi, Brik, Ashraf, and Wolberger, Cynthia. 2016.
"Structural basis for histone H2B deubiquitination by the SAGA DUB module". United States. https://doi.org/10.1126/science.aac5681. https://www.osti.gov/servlets/purl/1249222.
@article{osti_1249222,
title = {Structural basis for histone H2B deubiquitination by the SAGA DUB module},
author = {Morgan, Michael T. and Haj-Yahya, Mahmood and Ringel, Alison E. and Bandi, Prasanthi and Brik, Ashraf and Wolberger, Cynthia},
abstractNote = {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.},
doi = {10.1126/science.aac5681},
url = {https://www.osti.gov/biblio/1249222},
journal = {Science},
issn = {0036-8075},
number = 6274,
volume = 351,
place = {United States},
year = {Fri Feb 12 00:00:00 EST 2016},
month = {Fri Feb 12 00:00:00 EST 2016}
}
Web of Science
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