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rdf:type |
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lifeskim:mentions |
umls-concept:C0019647,
umls-concept:C0024337,
umls-concept:C0036025,
umls-concept:C0205314,
umls-concept:C0439851,
umls-concept:C0679622,
umls-concept:C0936012,
umls-concept:C1167622,
umls-concept:C1518791,
umls-concept:C1552596,
umls-concept:C1709061,
umls-concept:C1947931
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pubmed:issue |
4
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pubmed:dateCreated |
2007-1-22
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pubmed:abstractText |
The PHD finger motif is a signature chromatin-associated motif that is found throughout eukaryotic proteomes. Here we have determined the histone methyl-lysine binding activity of the PHD fingers present within the Saccharomyces cerevisiae proteome. We provide evidence on the genomic scale that PHD fingers constitute a general class of effector modules for histone H3 trimethylated at lysine 4 (H3K4me3) and histone H3 trimethylated at lysine 36 (H3K36me3). Structural modeling of PHD fingers demonstrates a conserved mechanism for recognizing the trimethyl moiety and provides insight into the molecular basis of affinity for the different methyl-histone ligands. Together, our study suggests that a common function for PHD fingers is to transduce methyl-lysine events and sheds light on how a single histone modification can be linked to multiple biological outcomes.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-10638745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-10944586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-11498575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-12824332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-12930999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-14975312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-15027865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-15033350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-15457208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-15666348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-15970672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16143104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16415788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16581777,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16728974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16728976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16728977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16728978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16823438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16826231,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-16923967,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17142463-8254673
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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 |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:BedfordMark TMT,
pubmed-author:BriggsScott DSD,
pubmed-author:ChanSteve MSM,
pubmed-author:DavrazouFoteiniF,
pubmed-author:FingermanIan MIM,
pubmed-author:GozaniOrO,
pubmed-author:HoweLeAnnL,
pubmed-author:KachirskaiaIouliaI,
pubmed-author:KuoJen-Hao AJH,
pubmed-author:KutateladzeTatiana GTG,
pubmed-author:LakeAimeeA,
pubmed-author:LugovskoyAlexey AAA,
pubmed-author:MartinDavid G EDG,
pubmed-author:ShiXiaobingX,
pubmed-author:UtzPaul JPJ,
pubmed-author:WalterKay LKL
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2450-5
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:17142463-Amino Acid Motifs,
pubmed-meshheading:17142463-Amino Acid Sequence,
pubmed-meshheading:17142463-DNA-Binding Proteins,
pubmed-meshheading:17142463-Histones,
pubmed-meshheading:17142463-Homeodomain Proteins,
pubmed-meshheading:17142463-Lysine,
pubmed-meshheading:17142463-Methylation,
pubmed-meshheading:17142463-Molecular Sequence Data,
pubmed-meshheading:17142463-Protein Binding,
pubmed-meshheading:17142463-Protein Structure, Tertiary,
pubmed-meshheading:17142463-Proteome,
pubmed-meshheading:17142463-Saccharomyces cerevisiae,
pubmed-meshheading:17142463-Saccharomyces cerevisiae Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36.
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pubmed:affiliation |
Department of Biological Sciences, Stanford University, Stanford, California 94305, 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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