Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-5-23
pubmed:abstractText
The development of the Drosophila wing requires both scalloped and vestigial functions. Using a fusion between full-length Vestigial and the Scalloped TEA domain, the fusion protein can rescue scalloped wing mutations because within wing development, Scalloped and Vestigial cooperatively act as a transcription complex. Scalloped provides the necessary DNA binding function via the TEA domain and Vestigial promotes the activation of target genes. We also demonstrate that the putative nuclear localization signal contained in the TEA domain of Scalloped is likely responsible for the nuclear localization of Vestigial. The fusion protein is also capable of activating a known target gene of the native complex and thus represents a tool that will be helpful in rapidly identifying target genes of the Sd/Vg complex that are involved in wing differentiation. The functionality of the fusion suggests that only the TEA domain of Scalloped is critical for wing development and the rest of the protein (about 70%) is dispensable. This result is novel and should stimulate further studies of sd in other tissues in view of the fact that scalloped is a vital gene in Drosophila.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1526-954X
pubmed:author
pubmed:copyrightInfo
Copyright 2002 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
40-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
A Vestigial:Scalloped TEA domain chimera rescues the wing phenotype of a scalloped mutation in Drosophila melanogaster.
pubmed:affiliation
Department of Biological Sciences, University of Alberta, Edmonton, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't