Structural basis for histone H2B deubiquitination by the SAGA DUB module
Structural basis for histone H2B deubiquitination by the SAGA DUB module
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United States: American Association for the Advancement of Science
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Language
English
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United States: American Association for the Advancement of Science
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Contents
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 reveal...
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Full title
Structural basis for histone H2B deubiquitination by the SAGA DUB module
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4863942
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4863942
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ISSN
0036-8075,1095-9203
E-ISSN
1095-9203
DOI
10.1126/science.aac5681
