Source:http://linkedlifedata.com/resource/pubmed/id/20836566
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2010-11-5
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pubmed:abstractText |
An important issue in epigenetic research is to understand how the numerous methylation marks associated with histone and certain nonhistone proteins are recognized and interpreted by the hundreds of chromatin-binding modules (CBMs) in a cell to control chromatin state, gene expression, and other cellular functions. We have assembled a peptide chip that represents known and putative lysine methylation marks on histones and p53 and probed the chip for binding to a group of CBMs to obtain a comprehensive interaction network mediated by lysine methylation. Interactions revealed by the peptide array screening were validated by in-solution binding assays. This study not only recapitulated known interactions but also uncovered new ones. A novel heterochromatin protein 1 beta (HP1?) chromodomain-binding site on histone H3, H3K23me, was discovered from the peptide array screen and subsequently verified by mass spectrometry. Data from peptide pull-down and colocalization in cells suggest that, besides the H3K9me mark, H3K23me may play a role in facilitating the recruitment of HP1? to the heterochromatin. Extending the peptide array and mass spectrometric approach presented here to more histone marks and CBMs would eventually afford a comprehensive specificity and interaction map to aid epigenetic studies.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1535-3907
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pubmed:author |
pubmed-author:BedfordMark TMT,
pubmed-author:GalkaMarekM,
pubmed-author:HuangZhipingZ,
pubmed-author:IbergAimeeA,
pubmed-author:JiangXinfengX,
pubmed-author:LajoieGillesG,
pubmed-author:LiLeiL,
pubmed-author:LiShawn S CSS,
pubmed-author:LiuHuadongH,
pubmed-author:VossCourtneyC,
pubmed-author:WangZezhouZ
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pubmed:issnType |
Electronic
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pubmed:day |
5
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5827-36
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pubmed:meshHeading |
pubmed-meshheading:20836566-Epigenomics,
pubmed-meshheading:20836566-Histones,
pubmed-meshheading:20836566-Humans,
pubmed-meshheading:20836566-Lysine,
pubmed-meshheading:20836566-Methylation,
pubmed-meshheading:20836566-Protein Array Analysis,
pubmed-meshheading:20836566-Protein Binding,
pubmed-meshheading:20836566-Tumor Suppressor Protein p53
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pubmed:year |
2010
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pubmed:articleTitle |
Systematic identification of methyllysine-driven interactions for histone and nonhistone targets.
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pubmed:affiliation |
Department of Biochemistry, The University of Western Ontario, London, Ontario, N6A 5C1, Canada.
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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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