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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1995-1-24
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pubmed:abstractText |
We show that the presence of a regulatory cis-acting element that flanks the core octamer site and dictates selectivity in the response to Vmw65 (VP16), while dispensable for POU binding per se, induces a conformational alteration in the nature of the POU domain in the DNA complex. A single substitution in the flanking signal distorts the POU complex and without affecting overall POU binding prevents Vmw65 interaction. Alternatively, substitution of a residue in the homeodomain predicted to contact the GARAT region prevents its recognition even on a wild-type motif, causing a reversion to the DNA binding pattern seen on a cellular motif and at the same time inefficient recognition by Vmw65. The results indicate that Vmw65 recognizes a particular POU domain conformation induced by the presence of the flanking GARAT region.
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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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HCFC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Herpes Simplex Virus Protein Vmw65,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Host Cell Factor C1,
http://linkedlifedata.com/resource/pubmed/chemical/Octamer Transcription Factor-1,
http://linkedlifedata.com/resource/pubmed/chemical/POU Domain Factors,
http://linkedlifedata.com/resource/pubmed/chemical/POU2F1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
841-52
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8001121-Base Sequence,
pubmed-meshheading:8001121-DNA,
pubmed-meshheading:8001121-DNA-Binding Proteins,
pubmed-meshheading:8001121-HeLa Cells,
pubmed-meshheading:8001121-Herpes Simplex Virus Protein Vmw65,
pubmed-meshheading:8001121-Homeodomain Proteins,
pubmed-meshheading:8001121-Host Cell Factor C1,
pubmed-meshheading:8001121-Humans,
pubmed-meshheading:8001121-Models, Molecular,
pubmed-meshheading:8001121-Molecular Sequence Data,
pubmed-meshheading:8001121-Nucleic Acid Conformation,
pubmed-meshheading:8001121-Octamer Transcription Factor-1,
pubmed-meshheading:8001121-POU Domain Factors,
pubmed-meshheading:8001121-Protein Binding,
pubmed-meshheading:8001121-Protein Conformation,
pubmed-meshheading:8001121-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:8001121-Structure-Activity Relationship,
pubmed-meshheading:8001121-Transcription, Genetic,
pubmed-meshheading:8001121-Transcription Factors,
pubmed-meshheading:8001121-Transcriptional Activation
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pubmed:year |
1994
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pubmed:articleTitle |
Site-specific conformational alteration of the Oct-1 POU domain-DNA complex as the basis for differential recognition by Vmw65 (VP16).
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pubmed:affiliation |
Marie Curie Research Institute, Oxted, Surrey, England.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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