rdf:type |
|
lifeskim:mentions |
umls-concept:C0013138,
umls-concept:C0024660,
umls-concept:C0086222,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C1512131,
umls-concept:C1521761,
umls-concept:C1521991,
umls-concept:C1534709,
umls-concept:C1552599,
umls-concept:C1704787,
umls-concept:C1705733,
umls-concept:C1880022
|
pubmed:issue |
3
|
pubmed:dateCreated |
1993-9-17
|
pubmed:databankReference |
|
pubmed:abstractText |
Drosophila hairy (h) plays a crucial role in early development as a pair-rule segmentation gene. h and its structurally related gene Enhancer of split [E(spl)] are also required for normal sensory neurogenesis in late development. To analyze the molecular mechanisms of mammalian development, we recently characterized three rat helix-loop-helix (HLH) factors that show structural homology to the Drosophila h and E(spl) gene products, and found that rat factors exhibit distinct spatiotemporal expression patterns and act as a negative regulator. Here, we report the molecular characterization of another member of this family, designated HES-2. Rat HES-2 protein has a basic HLH domain homologous to h and E(spl) as well as the carboxy-terminal Trp-Arg-Pro-Trp sequence conserved among this family. The HES-2 mRNA is present as early as embryonic day 9.5 and is detected in a variety of tissues of both embryos and adults. DNase-I-footprinting analyses indicate that HES-2 binds to all E box sequences (CANNTG) we tested as well as to the N-box sequences (CACNAG). Further studies of gel-mobility-shift assays show that HES-2 has a higher affinity for the E box than for the N box. Transient transfection analyses suggest that HES-2 decreases the transcription originating from the promoters containing either the E box or the N box. These results indicate that HES-2 acts as a negative regulator through interaction with both E-box and N-box sequences.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Basic Helix-Loop-Helix...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/hairy protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/hairy protein, insect
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0014-2956
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
215
|
pubmed:geneSymbol |
E(spl),
HES-2
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
645-52
|
pubmed:dateRevised |
2007-7-23
|
pubmed:meshHeading |
pubmed-meshheading:8354270-3T3 Cells,
pubmed-meshheading:8354270-Amino Acid Sequence,
pubmed-meshheading:8354270-Animals,
pubmed-meshheading:8354270-Base Sequence,
pubmed-meshheading:8354270-Basic Helix-Loop-Helix Transcription Factors,
pubmed-meshheading:8354270-Cloning, Molecular,
pubmed-meshheading:8354270-DNA,
pubmed-meshheading:8354270-DNA-Binding Proteins,
pubmed-meshheading:8354270-Drosophila,
pubmed-meshheading:8354270-Drosophila Proteins,
pubmed-meshheading:8354270-Insect Hormones,
pubmed-meshheading:8354270-Insect Proteins,
pubmed-meshheading:8354270-Mice,
pubmed-meshheading:8354270-Molecular Sequence Data,
pubmed-meshheading:8354270-RNA, Messenger,
pubmed-meshheading:8354270-Rats,
pubmed-meshheading:8354270-Repressor Proteins,
pubmed-meshheading:8354270-Sequence Homology, Amino Acid,
pubmed-meshheading:8354270-Transcription, Genetic,
pubmed-meshheading:8354270-Transcription Factors
|
pubmed:year |
1993
|
pubmed:articleTitle |
Molecular characterization of HES-2, a mammalian helix-loop-helix factor structurally related to Drosophila hairy and Enhancer of split.
|
pubmed:affiliation |
Institute for Immunology, Kyoto University Faculty of Medicine, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|