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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1999-5-25
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pubmed:abstractText |
Chromatin organization plays a key role in the regulation of gene expression. The evolutionarily conserved SWI/SNF complex is one of several multiprotein complexes that activate transcription by remodelling chromatin in an ATP-dependent manner. SWI2/SNF2 is an ATPase whose homologues, BRG1 and hBRM, mediate cell-cycle arrest; the SNF5 homologue, INI1/hSNF5, appears to be a tumour suppressor. A search for INI1-interacting proteins using the two-hybrid system led to the isolation of c-MYC, a transactivator. The c-MYC-INI1 interaction was observed both in vitro and in vivo. The c-MYC basic helix-loop-helix (bHLH) and leucine zipper (Zip) domains and the INI1 repeat 1 (Rpt1) region were required for this interaction. c-MYC-mediated transactivation was inhibited by a deletion fragment of INI1 and the ATPase mutant of BRG1/hSNF2 in a dominant-negative manner contingent upon the presence of the c-MYC bHLH-Zip domain. Our results suggest that the SWI/SNF complex is necessary for c-MYC-mediated transactivation and that the c-MYC-INI1 interaction helps recruit the complex.
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pubmed:grant |
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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/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoprotein, U1 Small Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCA4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/snf protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1061-4036
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
102-5
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10319872-Binding Sites,
pubmed-meshheading:10319872-Cell Line,
pubmed-meshheading:10319872-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:10319872-DNA Helicases,
pubmed-meshheading:10319872-DNA-Binding Proteins,
pubmed-meshheading:10319872-Drosophila Proteins,
pubmed-meshheading:10319872-HL-60 Cells,
pubmed-meshheading:10319872-HeLa Cells,
pubmed-meshheading:10319872-Humans,
pubmed-meshheading:10319872-Mutation,
pubmed-meshheading:10319872-Nuclear Proteins,
pubmed-meshheading:10319872-Protein Binding,
pubmed-meshheading:10319872-Protein Structure, Tertiary,
pubmed-meshheading:10319872-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:10319872-RNA-Binding Proteins,
pubmed-meshheading:10319872-Ribonucleoprotein, U1 Small Nuclear,
pubmed-meshheading:10319872-Transcription Factors,
pubmed-meshheading:10319872-Transcriptional Activation
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pubmed:year |
1999
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pubmed:articleTitle |
c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function.
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pubmed:affiliation |
Department of Molecular Genetics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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