Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
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
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