Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12A
pubmed:dateCreated
1993-1-13
pubmed:abstractText
Recently, we reported the cloning of the Drosophila melanogaster homolog of the vertebrate CCAAT/enhancer-binding protein (C/EBP). Here, we describe studies of the DNA-binding and dimerization properties of Drosophila C/EBP (DmC/EBP), as well as its tissue distribution, developmental regulation, and essential role in embryonic development and conclude that it bears functional as well as structural similarity to mammalian C/EBP. DmC/EBP contains a basic region/leucine zipper (bZIP) DNA-binding domain very similar to that of mammalian C/EBP and the purified C/EBPs bound to DNA with the same sequence specificity. Among the DNA sequences that DmC/EBP bound with high affinity was a conserved site within the promoter of the DmC/EBP gene itself. In vitro, DmC/EBP and mammalian C/EBP specifically formed functional heterodimers; however, as we found no evidence for a family of DmC/EBPs, DmC/EBP may function as a homodimer in vivo. The DmC/EBP protein was expressed predominantly during late embryogenesis in the nuclei of a restricted set of differentiating cell types, such as the lining of the gut and epidermis, similar to the mammalian tissues that express C/EBP. We have characterized mutations in the DmC/EBP gene and found that deleting the gene caused late embryonic lethality. Embryos that lack C/EBP die just before or just upon hatching. The lethal phenotype of C/EBP mutants can be rescued with the cloned C/EBP gene introduced by P-element-mediated germ-line transformation. The strict requirement for C/EBP during Drosophila embryogenesis, coupled with its structural and functional similarities to mammalian C/EBP, provides a useful genetic system in which to study the role of C/EBP in development.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2299-311
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:1459454-Amino Acid Sequence, pubmed-meshheading:1459454-Animals, pubmed-meshheading:1459454-Base Sequence, pubmed-meshheading:1459454-Blotting, Northern, pubmed-meshheading:1459454-CCAAT-Enhancer-Binding Proteins, pubmed-meshheading:1459454-Cloning, Molecular, pubmed-meshheading:1459454-DNA, pubmed-meshheading:1459454-DNA-Binding Proteins, pubmed-meshheading:1459454-Drosophila melanogaster, pubmed-meshheading:1459454-Escherichia coli, pubmed-meshheading:1459454-Germ Cells, pubmed-meshheading:1459454-Molecular Sequence Data, pubmed-meshheading:1459454-Nuclear Proteins, pubmed-meshheading:1459454-Organ Specificity, pubmed-meshheading:1459454-Promoter Regions, Genetic, pubmed-meshheading:1459454-Protein Binding, pubmed-meshheading:1459454-Restriction Mapping, pubmed-meshheading:1459454-Sequence Homology, Amino Acid, pubmed-meshheading:1459454-Transcription Factors, pubmed-meshheading:1459454-Transformation, Genetic
pubmed:year
1992
pubmed:articleTitle
Drosophila C/EBP: a tissue-specific DNA-binding protein required for embryonic development.
pubmed:affiliation
Howard Hughes Research Laboratory, Department of Embryology, Carnegie Institution of Washington, Baltimore, Maryland 21210.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't