Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6285
pubmed:dateCreated
1990-9-17
pubmed:abstractText
The human muscle determination factor myf5, like MyoD and other members of the family of skeletal muscle-specific regulatory proteins, contains a highly conserved putative helix-loop-helix domain. In MyoD this motif is required for the initiation of myogenesis in C3H mouse 10T1/2 fibroblasts and other non-muscle cells as well as for transcriptional activation of muscle genes. High affinity DNA binding of MyoD to regulatory DNA elements in muscle genes requires the formation of heterodimers with ubiquitous helix-loop-helix proteins such as E12 or E47. To investigate the potential of myf5 as a transcription factor, we have fused the GAL4 DNA-binding domain to various parts of the myf5 protein and analysed the transactivation of a GAL4 reporter plasmid. Here we report that myf5 contains an intrinsic transcriptional activation domain which is distinct from the helix-loop-helix motif. The predominant transactivating effect is associated with the C-terminal half of the myf5 molecule. High-affinity sequence-specific DNA binding of myf5 also requires hetero-oligomeric association with the enhancer-binding protein E12 to confer muscle-specific transactivation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Chloramphenicol O-Acetyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GAL4 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/MYF5 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Myf5 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Myogenic Regulatory Factor 5, http://linkedlifedata.com/resource/pubmed/chemical/Myosins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
346
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
663-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:2385294-Animals, pubmed-meshheading:2385294-Binding Sites, pubmed-meshheading:2385294-Cell Line, pubmed-meshheading:2385294-Chloramphenicol O-Acetyltransferase, pubmed-meshheading:2385294-DNA, pubmed-meshheading:2385294-DNA-Binding Proteins, pubmed-meshheading:2385294-Fibroblasts, pubmed-meshheading:2385294-Fungal Proteins, pubmed-meshheading:2385294-HeLa Cells, pubmed-meshheading:2385294-Humans, pubmed-meshheading:2385294-Mice, pubmed-meshheading:2385294-Muscle Proteins, pubmed-meshheading:2385294-Myogenic Regulatory Factor 5, pubmed-meshheading:2385294-Myosins, pubmed-meshheading:2385294-Plasmids, pubmed-meshheading:2385294-Promoter Regions, Genetic, pubmed-meshheading:2385294-Protein Conformation, pubmed-meshheading:2385294-Recombinant Fusion Proteins, pubmed-meshheading:2385294-Saccharomyces cerevisiae Proteins, pubmed-meshheading:2385294-Trans-Activators, pubmed-meshheading:2385294-Transcription, Genetic, pubmed-meshheading:2385294-Transcription Factors, pubmed-meshheading:2385294-Transcriptional Activation, pubmed-meshheading:2385294-Transfection
pubmed:year
1990
pubmed:articleTitle
Transcriptional activation domain of the muscle-specific gene-regulatory protein myf5.
pubmed:affiliation
Department of Toxicology, Medical School, University of Hamburg, FRG.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't