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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
30
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pubmed:dateCreated |
2004-7-1
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pubmed:abstractText |
The E2F family of transcription factors play an important role in regulating cell cycle progression. We report here the characterization and functional properties of a new member of the human E2F family, referred to as E2F-7. E2F-7 has two separate DNA-binding domains, a feature that distinguishes E2F-7 from other mammalian E2F proteins, but resembling the organization of recently isolated E2F-like proteins from Arabidopsis. E2F-7 binds to DNA independently of a DP partner and delays cell cycle progression. Interestingly, E2F-7 modulates the transcription properties of other E2F proteins. A mutational analysis indicates that the integrity of both DNA-binding domains is required for cell cycle delay and transcriptional modulation. Biochemical results and protein modelling studies suggest that in binding to DNA interactions occur between the two DNA-binding domains, most probably as a homodimer, thereby mimicking the organization of an E2F/DP heterodimer. These structural and functional properties of E2F-7 imply a unique role in regulating cellular proliferation.
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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 |
Jul
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pubmed:issn |
0950-9232
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5138-50
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15133492-Amino Acid Motifs,
pubmed-meshheading:15133492-Amino Acid Sequence,
pubmed-meshheading:15133492-Binding Sites,
pubmed-meshheading:15133492-Cell Cycle,
pubmed-meshheading:15133492-Cell Line, Tumor,
pubmed-meshheading:15133492-Cell Nucleus,
pubmed-meshheading:15133492-Conserved Sequence,
pubmed-meshheading:15133492-DNA-Binding Proteins,
pubmed-meshheading:15133492-E2F7 Transcription Factor,
pubmed-meshheading:15133492-Genes, Reporter,
pubmed-meshheading:15133492-HeLa Cells,
pubmed-meshheading:15133492-Humans,
pubmed-meshheading:15133492-Luciferases,
pubmed-meshheading:15133492-Models, Molecular,
pubmed-meshheading:15133492-Molecular Sequence Data,
pubmed-meshheading:15133492-Mutagenesis, Site-Directed,
pubmed-meshheading:15133492-Mutation,
pubmed-meshheading:15133492-Precipitin Tests,
pubmed-meshheading:15133492-Protein Binding,
pubmed-meshheading:15133492-Protein Structure, Tertiary,
pubmed-meshheading:15133492-Repressor Proteins,
pubmed-meshheading:15133492-Sequence Homology, Amino Acid,
pubmed-meshheading:15133492-Transcription Factors
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pubmed:year |
2004
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pubmed:articleTitle |
E2F-7: a distinctive E2F family member with an unusual organization of DNA-binding domains.
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pubmed:affiliation |
Division of Biochemistry and Molecular Biology, Davidson Building, University of Glasgow, Glasgow, G12 8QQ, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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