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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2006-5-22
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pubmed:abstractText |
Jun dimerization protein-2 (JDP2) is a component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Here, we examine the functional mechanisms of JDP2 and show that it can inhibit p300-mediated acetylation of core histones in vitro and in vivo. Inhibition of histone acetylation requires the N-terminal 35 residues and the DNA-binding region of JDP2. In addition, we demonstrate that JDP2 has histone-chaperone activity in vitro. These results suggest that the sequence-specific DNA-binding protein JDP2 may control transcription via direct regulation of the modification of histones and the assembly of chromatin.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Jundp2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosomes,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP-associated factor
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1545-9993
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pubmed:author |
pubmed-author:ChimuraTakahikoT,
pubmed-author:ChiuRobertR,
pubmed-author:HorikoshiMasamiM,
pubmed-author:ItoTakashiT,
pubmed-author:JinChunyuanC,
pubmed-author:KatoKohsukeK,
pubmed-author:LiHongjieH,
pubmed-author:MurataTakehideT,
pubmed-author:NagataKyosukeK,
pubmed-author:NakadeKojiK,
pubmed-author:PanJianzhiJ,
pubmed-author:SunKailaiK,
pubmed-author:YamasakiTakahitoT,
pubmed-author:YokoyamaKazunari KKK,
pubmed-author:ZhaoMujunM
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
331-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16518400-Acetylation,
pubmed-meshheading:16518400-Animals,
pubmed-meshheading:16518400-Base Sequence,
pubmed-meshheading:16518400-Cell Cycle Proteins,
pubmed-meshheading:16518400-DNA,
pubmed-meshheading:16518400-HeLa Cells,
pubmed-meshheading:16518400-Histone Acetyltransferases,
pubmed-meshheading:16518400-Histones,
pubmed-meshheading:16518400-Humans,
pubmed-meshheading:16518400-Mice,
pubmed-meshheading:16518400-Molecular Chaperones,
pubmed-meshheading:16518400-Nucleosomes,
pubmed-meshheading:16518400-Protein Binding,
pubmed-meshheading:16518400-Protein Structure, Tertiary,
pubmed-meshheading:16518400-Recombinant Proteins,
pubmed-meshheading:16518400-Repressor Proteins,
pubmed-meshheading:16518400-Sequence Deletion,
pubmed-meshheading:16518400-Transcription Factors,
pubmed-meshheading:16518400-p300-CBP Transcription Factors
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pubmed:year |
2006
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pubmed:articleTitle |
Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2.
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pubmed:affiliation |
Gene Engineering Division, Dept. of Biological Systems, BioResource Center, RIKEN (The Institute of Physical & Chemical Research), Tsukuba Science City, Ibaraki 305-0074, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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