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rdf:type |
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lifeskim:mentions |
umls-concept:C0013138,
umls-concept:C0019647,
umls-concept:C0024337,
umls-concept:C0025723,
umls-concept:C0033684,
umls-concept:C1257890,
umls-concept:C1426004,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1709915
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pubmed:issue |
20
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pubmed:dateCreated |
2003-10-1
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pubmed:abstractText |
Covalent modifications of histone tails modulate gene expression via chromatin organization. As examples, methylation of lysine 9 residues of histone H3 (H3) (H3-K9) is believed to repress transcription by compacting chromatin, whereas methylation of lysine 4 residues of H3 (H3-K4) is believed to activate transcription by relaxing chromatin. The Drosophila trithorax group protein absent, small, or homeotic discs 1 (ASH1) is involved in maintaining active transcription of many genes. Here we report that in extreme ash1 mutants, no H3-K4 methylation is detectable. Within the limits of our assays, this lack of detectable H3-K4 methylation implies that ASH1 is required for essentially all H3-K4 methylation that occurs in vivo. We report further that the 149-aa SET domain of ASH1 is sufficient for H3-K4 methylation in vitro. These findings support a model in which ASH1 is directly involved in maintaining active transcription by conferring a relaxed chromatin structure.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-10454589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-10611321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-10638722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-10949293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-11114889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-11316813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-11544176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-11701926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-11850410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-11867540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-12353038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-12397363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-12670868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-14114491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-2497049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-7915232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-7958911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-7982557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/13679578-8725238
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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 |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
100
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11535-40
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2003
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pubmed:articleTitle |
ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3.
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pubmed:affiliation |
Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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