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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12B
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pubmed:dateCreated |
1993-12-1
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pubmed:databankReference | |
pubmed:abstractText |
We report the molecular characterization of two novel rat helix-loop-helix (HLH) proteins, designated HES-1 and HES-3, that show structural homology to the Drosophila hairy and Enhancer of split [E(spl)] proteins, both of which are required for normal neurogenesis. HES-1 mRNA, expressed in various tissues of both embryos and adults, is present at a high level in the epithelial cells, including the embryonal neuroepithelial cells, as well as in the mesoderm-derived tissues such as the embryonal muscle. In contrast, HES-3 mRNA is produced exclusively in cerebellar Purkinje cells. HES-1 represses transcription by binding to the N box, which is a recognition sequence of E(spl) proteins. Interestingly, neither HES-1 nor HES-3 alone interacts efficiently with the E box, but each protein decreases the transcription induced by E-box-binding HLH activators such as E47. Furthermore, HES-1 also inhibits the functions of MyoD and MASH1 and effectively diminishes the myogenic conversion of C3H10T1/2 cells induced by MyoD. These results suggest that HES-1 may play an important role in mammalian development by negatively acting on the two different sequences while HES-3 acts as a repressor in a specific type of neurons.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0890-9369
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pubmed:author | |
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 |
2620-34
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1340473-Amino Acid Sequence,
pubmed-meshheading:1340473-Animals,
pubmed-meshheading:1340473-Base Sequence,
pubmed-meshheading:1340473-Basic Helix-Loop-Helix Transcription Factors,
pubmed-meshheading:1340473-DNA,
pubmed-meshheading:1340473-DNA-Binding Proteins,
pubmed-meshheading:1340473-Drosophila,
pubmed-meshheading:1340473-Helix-Loop-Helix Motifs,
pubmed-meshheading:1340473-Homeodomain Proteins,
pubmed-meshheading:1340473-In Situ Hybridization,
pubmed-meshheading:1340473-Male,
pubmed-meshheading:1340473-Molecular Sequence Data,
pubmed-meshheading:1340473-Polymerase Chain Reaction,
pubmed-meshheading:1340473-Rats,
pubmed-meshheading:1340473-Rats, Sprague-Dawley,
pubmed-meshheading:1340473-Sequence Homology, Amino Acid
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pubmed:year |
1992
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pubmed:articleTitle |
Two mammalian helix-loop-helix factors structurally related to Drosophila hairy and Enhancer of split.
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pubmed:affiliation |
Institute for Immunology, Kyoto University Faculty of Medicine, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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