Abstract
The double-stranded RNA (dsRNA)-binding domain of the human p68 kinase has been localized to the N-terminal half of the enzyme by using progressive deletion analysis and in vitro binding assays. To further define the domains responsible for binding to dsRNA, we cloned the mouse dsRNA-activated p65 kinase and used sequence alignment to identify conserved domains in the N-terminal region. Deletions in either of two 12-amino-acid-long and arginine- or lysine-rich regions abrogated binding to dsRNA. Moreover, in an in vivo growth inhibition assay in the yeast Saccharomyces cerevisiae, these mutants failed to exhibit a slow-growth phenotype.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Binding Sites
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Cell Line
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Chromosome Deletion
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Cloning, Molecular
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Enzyme Activation
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Enzyme Induction
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Humans
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Mice
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Poly I-C / metabolism
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Protein Biosynthesis
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Protein Kinases / genetics*
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Protein Kinases / metabolism*
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RNA, Double-Stranded / metabolism*
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / growth & development
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Sequence Homology, Nucleic Acid
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Transcription, Genetic
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eIF-2 Kinase
Substances
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RNA, Double-Stranded
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Protein Kinases
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eIF-2 Kinase
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Poly I-C