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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2010-5-3
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pubmed:abstractText |
The Polybromo (PB) protein functions as a key component of the human PBAF chromatin remodeling complex in regulation of gene transcription. PB is made up of modular domains including six bromodomains that are known as acetyl-lysine binding domains. However, histone-binding specificity of the bromodomains of PB has remained elusive. In this study, we report biochemical characterization of all six PB bromodomains' binding to a suite of lysine-acetylated peptides derived from known acetylation sites on human core histones. We demonstrate that bromodomain 2 of PB preferentially recognizes acetylated lysine 14 of histone H3 (H3K14ac), a post-translational mark known for gene transcriptional activation. We further describe the molecular basis of the selective H3K14ac recognition of bromodomain 2 by solving the protein structures in both the free and bound forms using X-ray crystallography and NMR, respectively.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-10365964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-11290320,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-11368894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-11911891,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-16537902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-16648632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-16728978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-16829979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-16916647,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-17803945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-17984965,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-18400184,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-18508041,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-18837912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-18978020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-19084573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-19160500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-19596240,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-19794495,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-8917104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-9008363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20368734-9757107
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1748-7838
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
529-38
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pubmed:dateRevised |
2011-6-2
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pubmed:meshHeading |
pubmed-meshheading:20368734-Amino Acid Sequence,
pubmed-meshheading:20368734-Crystallography, X-Ray,
pubmed-meshheading:20368734-Histones,
pubmed-meshheading:20368734-Humans,
pubmed-meshheading:20368734-Models, Molecular,
pubmed-meshheading:20368734-Molecular Sequence Data,
pubmed-meshheading:20368734-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:20368734-Nuclear Proteins,
pubmed-meshheading:20368734-Protein Binding,
pubmed-meshheading:20368734-Protein Conformation,
pubmed-meshheading:20368734-Protein Structure, Tertiary,
pubmed-meshheading:20368734-Transcription Factors
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pubmed:year |
2010
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pubmed:articleTitle |
Structural insights into selective histone H3 recognition by the human Polybromo bromodomain 2.
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pubmed:affiliation |
Department of Structural and Chemical Biology, Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, NY 10029, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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