rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
51
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pubmed:dateCreated |
2010-12-23
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pubmed:abstractText |
Ig class switch recombination (CSR) requires expression of activation-induced cytidine deaminase (AID) and transcription through target switch (S) regions. Here we show that knockdown of the histone chaperone facilitates chromatin transcription (FACT) completely inhibited S region cleavage and CSR in IgA-switch-inducible CH12F3-2A B cells. FACT knockdown did not reduce AID or S region transcripts but did decrease histone3 lysine4 trimethylation (H3K4me3) at both the S? and S? regions. Because knockdown of FACT or H3K4 methyltransferase cofactors inhibited DNA cleavage in H3K4me3-depleted S regions, H3K4me3 may serve as a mark for recruiting CSR recombinase. These findings revealed an unexpected evolutionary conservation between CSR and meiotic recombination.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21139053-10199952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21139053-10458604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21139053-10891502,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21139053-8671604
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AICDA (activation-induced cytidine...,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Cytidine Deaminase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Ssrp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/VDJ Recombinases
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
|
pubmed:issn |
1091-6490
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:day |
21
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pubmed:volume |
107
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
22190-5
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pubmed:dateRevised |
2011-8-1
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pubmed:meshHeading |
pubmed-meshheading:21139053-Animals,
pubmed-meshheading:21139053-B-Lymphocytes,
pubmed-meshheading:21139053-Cell Line,
pubmed-meshheading:21139053-Chromatin,
pubmed-meshheading:21139053-Cytidine Deaminase,
pubmed-meshheading:21139053-DNA,
pubmed-meshheading:21139053-DNA-Binding Proteins,
pubmed-meshheading:21139053-Evolution, Molecular,
pubmed-meshheading:21139053-High Mobility Group Proteins,
pubmed-meshheading:21139053-Histones,
pubmed-meshheading:21139053-Immunoglobulin Class Switching,
pubmed-meshheading:21139053-Lysine,
pubmed-meshheading:21139053-Meiosis,
pubmed-meshheading:21139053-Methylation,
pubmed-meshheading:21139053-Mice,
pubmed-meshheading:21139053-Transcription, Genetic,
pubmed-meshheading:21139053-VDJ Recombinases
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pubmed:year |
2010
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pubmed:articleTitle |
Histone3 lysine4 trimethylation regulated by the facilitates chromatin transcription complex is critical for DNA cleavage in class switch recombination.
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pubmed:affiliation |
Department of Immunology and Genomic Medicine, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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