Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI

Green, S. R., Mathews, M. B. (December 1992) Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI. Genes Dev, 6 (12B). pp. 2478-90. ISSN 0890-9369 (Print)0890-9369 (Linking)

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URL: http://www.ncbi.nlm.nih.gov/pubmed/1364113
DOI: 10.1101/gad.6.12b.2478

Abstract

The protein kinase DAI, the double-stranded RNA-activated inhibitor of translation, is an essential component of the interferon-induced cellular antiviral response. The enzyme is regulated by the binding of activator and inhibitor RNAs. We synthesized DAI in vitro and located its RNA-binding domain within the amino-terminal 171 residues. This domain contains two copies of an RNA-binding motif characterized by a high density of basic amino acids, by the presence of conserved residues, and by a probable alpha-helical structure. Deletion of either of the two motifs prevents the binding of dsRNA, but their relative positions can be exchanged, suggesting that they cooperate to interact with dsRNA. Clustered point mutations within the RNA-binding motifs and duplications of the individual motifs indicate that the first copy of the motif plays the more important role. Mutations that impair binding have similar effects on the binding of double-stranded RNAs of various lengths and of adenovirus VA RNAI, implying that discrimination between activator and inhibitory RNAs takes place subsequent to RNA binding.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Enzyme Activation Molecular Sequence Data Mutagenesis Point Mutation Protein Biosynthesis Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism RNA, Double-Stranded/*metabolism eIF-2 Kinase
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > dsRNA
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > RNA binding protein
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: December 1992
Date Deposited: 01 Oct 2015 16:38
Last Modified: 03 Nov 2017 20:44
Related URLs:
URI: http://repository.cshl.edu/id/eprint/31795

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