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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0026845,
umls-concept:C0033684,
umls-concept:C0035820,
umls-concept:C0040300,
umls-concept:C0040649,
umls-concept:C0086222,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C1167622,
umls-concept:C1420679,
umls-concept:C1522492,
umls-concept:C1552599,
umls-concept:C1704241,
umls-concept:C1704787,
umls-concept:C1705733
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pubmed:issue |
14
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pubmed:dateCreated |
1996-6-21
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pubmed:abstractText |
M-CAT sites are required for the activity of many promoters in cardiac and skeletal muscle. M-CAT binding activity is muscle-enriched, but is found in many tissues and is immunologically related to the HeLa transcription enhancer factor-1 (TEF-1). TEF-1-related cDNAs (RTEF-1) have been cloned from chick heart. RTEF-1 mRNA is muscle-enriched, consistent with a role for RTEF-1 in the regulation of muscle-specific gene expression. Here, we have examined the tissue distribution of TEF-1-related proteins and of M-CAT binding activity by Western analysis and mobility shift polyacrylamide gel electrophoresis. TEF-1-related proteins of 57, 54 and 52 kDa were found in most tissues with the highest levels in muscle tissues. All of these TEF-1-related proteins bound M-CAT DNA and the 57- and 54-kDa TEF-1-related polypeptides were phosphorylated. Proteolytic digestion mapping showed that the 54-kDa TEF-1-related polypeptide is encoded by a different gene than the 52- and 57-kDa TEF-1-related polypeptides. A comparison of the migration and proteolytic digestion of the 54-kDa TEF-1-related polypeptide with proteins encoded by the cloned RTEF-1 cDNAs showed that the 54-kDa TEF-1-related polypeptide is encoded by RTEF-1A. High resolution mobility shift polyacrylamide gel electrophoresis showed multiple M-CAT binding activities in tissues. All of these activities contained TEF-1-related proteins. One protein-M-CAT DNA complex was muscle-enriched and was up-regulated upon differentiation of a skeletal muscle cell line. This complex contained the 54-kDa TEF-1-related polypeptide. Therefore, RTEF1-A protein is a component of a muscle-enriched transcription complex that forms on M-CAT sites and may play a key role in the regulation of transcription in muscle.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/TEAD1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8266-74
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:8626521-Amino Acid Sequence,
pubmed-meshheading:8626521-Animals,
pubmed-meshheading:8626521-Chickens,
pubmed-meshheading:8626521-DNA-Binding Proteins,
pubmed-meshheading:8626521-Gene Expression Regulation,
pubmed-meshheading:8626521-Genes,
pubmed-meshheading:8626521-Immunologic Techniques,
pubmed-meshheading:8626521-Molecular Sequence Data,
pubmed-meshheading:8626521-Molecular Weight,
pubmed-meshheading:8626521-Multigene Family,
pubmed-meshheading:8626521-Muscles,
pubmed-meshheading:8626521-Nuclear Proteins,
pubmed-meshheading:8626521-Peptide Mapping,
pubmed-meshheading:8626521-Phosphoproteins,
pubmed-meshheading:8626521-Phosphorylation,
pubmed-meshheading:8626521-Promoter Regions, Genetic,
pubmed-meshheading:8626521-Regulatory Sequences, Nucleic Acid,
pubmed-meshheading:8626521-Tissue Distribution,
pubmed-meshheading:8626521-Transcription Factors
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pubmed:year |
1996
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pubmed:articleTitle |
The role of transcription enhancer factor-1 (TEF-1) related proteins in the formation of M-CAT binding complexes in muscle and non-muscle tissues.
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pubmed:affiliation |
Department of Anatomy and Cardiovascular Research Institute, University of California, San Francisco, 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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