title: A conserved double-stranded RNA-binding domain.
abstract: We have identified a double-stranded (ds)RNA-binding domain in each of two proteins: the product of the Drosophila gene staufen, which is required for the localization of maternal mRNAs, and a protein of unknown function, Xlrbpa, from Xenopus. The amino acid sequences of the binding domains are similar to each other and to additional domains in each protein. Database searches identified similar domains in several other proteins known or thought to bind dsRNA, including human dsRNA-activated inhibitor (DAI), human trans-activating region (TAR)-binding protein, and Escherichia coli RNase III. By analyzing in detail one domain in staufen and one in Xlrbpa, we delimited the minimal region that binds dsRNA. On the basis of the binding studies and computer analysis, we have derived a consensus sequence that defines a 65- to 68-amino acid dsRNA-binding domain.
authors.affiliation: Wellcome/Cancer Research Campaign Institute, Cambridge, United Kingdom.
authors.forename: D
authors.initials: D
authors.lastname: St Johnston
authors.forename: N H
authors.initials: NH
authors.lastname: Brown
authors.forename: J G
authors.initials: JG
authors.lastname: Gall
authors.forename: M
authors.initials: M
authors.lastname: Jantsch
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D003001:Cloning, Molecular; D016208:Databases, Factual; D004331:Drosophila melanogaster / Q000235:genetics / Q000378:metabolism; D005260:Female; D015723:Gene Library; D006801:Humans; D008969:Molecular Sequence Data; D010053:Ovary / Q000378:metabolism; D012330:RNA, Double-Stranded / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D014982:Xenopus laevis
chemical_list: D012330:RNA, Double-Stranded; D016601:RNA-Binding Proteins; D011993:Recombinant Fusion Proteins