A Conserved Double-Stranded RNA-Binding Domain

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 simi...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1992-11, Vol.89 (22), p.10979-10983
Main Authors: St Johnston, Daniel, Brown, Nicholas H., Gall, Joseph G., Jantsch, Michael
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Analytical, structural and metabolic biochemistry
Animals
Binding and carrier proteins
Binding Sites
Biochemistry
Biological and medical sciences
Biological Evolution
Cloning, Molecular
Complementary DNA
Consensus sequence
Databases, Factual
Double stranded RNA
Drosophila
Drosophila melanogaster - genetics
Drosophila melanogaster - metabolism
Female
Fundamental and applied biological sciences. Psychology
Gene Library
Humans
Molecular Sequence Data
Ovary - metabolism
Proteins
Recombinant Fusion Proteins - metabolism
Ribonucleic acid
RNA
RNA, Double-Stranded - metabolism
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
Rotavirus
Sequence Deletion
Sequence Homology, Amino Acid
Small nuclear RNA
Untranslated regions
Xenopus
Xenopus laevis
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Description
Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.89.22.10979