Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-3-9
pubmed:databankReference
pubmed:abstractText
The Drosophila gene vasa (vas) encodes an RNA-binding protein required for embryonic patterning and germ cell specification. In vas mutants, translation of several germline mRNAs is reduced. Here we show that VAS interacts directly with the Drosophila homolog of yeast translation initiation factor 2, encoded by a novel gene, dIF2. Embryos produced by vas/+; dIF2/+ females have pattern defects and fewer germline progenitor cells, indicating a functional interaction between endogenous vas and dIF2 activities. Mutations in other translation initiation factors do not enhance the vas phenotype, suggesting that dIF2 has a particular role in germ plasm function. We conclude that VAS regulates translation of germline mRNAs by specific interaction with dIF2, an essential factor conserved from bacteria to humans.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10678180-Amino Acid Sequence, pubmed-meshheading:10678180-Animals, pubmed-meshheading:10678180-DEAD-box RNA Helicases, pubmed-meshheading:10678180-Drosophila Proteins, pubmed-meshheading:10678180-Drosophila melanogaster, pubmed-meshheading:10678180-Eukaryotic Initiation Factor-2, pubmed-meshheading:10678180-Eukaryotic Initiation Factor-4A, pubmed-meshheading:10678180-Eukaryotic Initiation Factor-4E, pubmed-meshheading:10678180-Exons, pubmed-meshheading:10678180-Female, pubmed-meshheading:10678180-Heterozygote, pubmed-meshheading:10678180-Molecular Sequence Data, pubmed-meshheading:10678180-Mutation, pubmed-meshheading:10678180-Peptide Initiation Factors, pubmed-meshheading:10678180-RNA Helicases, pubmed-meshheading:10678180-Recombinant Proteins, pubmed-meshheading:10678180-Restriction Mapping, pubmed-meshheading:10678180-Saccharomyces cerevisiae, pubmed-meshheading:10678180-Sequence Alignment
pubmed:year
2000
pubmed:articleTitle
VASA mediates translation through interaction with a Drosophila yIF2 homolog.
pubmed:affiliation
Abteilung Molekulare Entwicklungsbiologie Max-Planck-Institut für biophysikalische Chemie, Göttingen, Germany.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't