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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1992-7-2
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pubmed:abstractText |
The ets gene family is composed of several oncogenes and codes for transcription factors. The Ets proteins have a similar sequence called the ets domain and bind to the core motif A/CGGAA. We show here that several members of the ets family have different trans-activating properties. The ets domain of Ets-1 is required for DNA binding. Adjacent to this domain there is a novel element that inhibits DNA binding. It appears to alter the structure of the DNA-binding domain before it interacts with DNA. There is a similar sequence in Ets-2 that also inhibits DNA binding. This sequence is absent in alternative splice products of h-Ets-1. PU1, the most distantly related member of the ets gene family, lacks this novel element. It has a distinct DNA-binding specificity that is determined by DNA sequences outside the core motif. These results have important implications for both the oncogenic and normal functions of ets family members.
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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/ERF protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ETS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ETS2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Protein c-ets-1,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Protein c-ets-2,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-ets,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0890-9369
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
965-74
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1592263-Amino Acid Sequence,
pubmed-meshheading:1592263-Base Sequence,
pubmed-meshheading:1592263-DNA,
pubmed-meshheading:1592263-DNA-Binding Proteins,
pubmed-meshheading:1592263-Humans,
pubmed-meshheading:1592263-Molecular Sequence Data,
pubmed-meshheading:1592263-Mutation,
pubmed-meshheading:1592263-Phosphorylation,
pubmed-meshheading:1592263-Precipitin Tests,
pubmed-meshheading:1592263-Protein Conformation,
pubmed-meshheading:1592263-Proto-Oncogene Protein c-ets-1,
pubmed-meshheading:1592263-Proto-Oncogene Protein c-ets-2,
pubmed-meshheading:1592263-Proto-Oncogene Proteins,
pubmed-meshheading:1592263-Proto-Oncogene Proteins c-ets,
pubmed-meshheading:1592263-Repressor Proteins,
pubmed-meshheading:1592263-Trans-Activators,
pubmed-meshheading:1592263-Transcription Factors,
pubmed-meshheading:1592263-Transcriptional Activation
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pubmed:year |
1992
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pubmed:articleTitle |
A novel modulator domain of Ets transcription factors.
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pubmed:affiliation |
Centre National de la Recherche Scientifique-Laboratoire de Génétique Moléculaire des Eucaryotes/Institut National de la Santé et de la Recherche Médicale (INSERM), Faculté de Médecine, Strasbourg, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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