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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
38
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pubmed:dateCreated |
2002-9-16
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pubmed:abstractText |
p21(SNFT) (21-kDa small nuclear factor isolated from T cells) is a novel human protein of the basic leucine zipper family. The overexpression of p21(SNFT) leads to the significant and specific repression of transcription from the interleukin-2 promoter as well as from several essential activator protein 1 (AP-1)-driven composite promoter elements. One example is the distal nuclear factor of activated T cells (NF-AT)/AP-1 element where the AP-1 (Fos/Jun) basic leucine zipper heterodimer interacts with members of the NF-AT family. p21(SNFT) has been shown to replace Fos in dimerization with Jun on a consensus AP-1 binding site (12-O-tetradecanolyphorbol-13-acetate response element (TRE)) and to interact with Jun and NF-AT at the distal NF-AT/AP-1 enhancer element. A detailed biochemical analysis presented here compares interactions involving p21(SNFT) with those involving Fos. The results demonstrate that a p21(SNFT)/Jun dimer binds a TRE similarly to AP-1 and like AP-1 binds cooperatively with NF-AT at the NF-AT/AP-1 composite element. However, Fos interacts significantly more efficiently than p21(SNFT) with Jun and NF-AT, and the replacement of Fos by p21(SNFT) in the trimolecular complex drastically alters protein-DNA contacts. The data suggest that p21(SNFT) may repress transcriptional activity by inducing a unique conformation in the transcription factor complex.
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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/Basic-Leucine Zipper Transcription...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NFATC Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-jun,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNFT protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
34967-77
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12087103-Basic-Leucine Zipper Transcription Factors,
pubmed-meshheading:12087103-Cell Nucleus,
pubmed-meshheading:12087103-DNA,
pubmed-meshheading:12087103-DNA Footprinting,
pubmed-meshheading:12087103-DNA-Binding Proteins,
pubmed-meshheading:12087103-Dimerization,
pubmed-meshheading:12087103-Enhancer Elements, Genetic,
pubmed-meshheading:12087103-Green Fluorescent Proteins,
pubmed-meshheading:12087103-HeLa Cells,
pubmed-meshheading:12087103-Humans,
pubmed-meshheading:12087103-Interleukin-2,
pubmed-meshheading:12087103-Luminescent Proteins,
pubmed-meshheading:12087103-NFATC Transcription Factors,
pubmed-meshheading:12087103-Nuclear Proteins,
pubmed-meshheading:12087103-Promoter Regions, Genetic,
pubmed-meshheading:12087103-Proto-Oncogene Proteins c-jun,
pubmed-meshheading:12087103-Recombinant Fusion Proteins,
pubmed-meshheading:12087103-Repressor Proteins,
pubmed-meshheading:12087103-Transcription, Genetic,
pubmed-meshheading:12087103-Transcription Factors
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pubmed:year |
2002
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pubmed:articleTitle |
Correlation of transcriptional repression by p21(SNFT) with changes in DNA.NF-AT complex interactions.
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pubmed:affiliation |
Department of Biology, San Diego State University, San Diego, California 92182-4614, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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