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Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p

  • BEIHUA DONG (a1), MAHO NIWA (a2), PETER WALTER (a2) and ROBERT H. SILVERMAN (a1)
  • Published online: 07 March 2001
Abstract

RNase L and Ire1p are members of a superfamily of regulated endoribonucleases that play essential roles in mediating diverse types of cellular stress responses. 2′-5′ oligoadenylates, produced in response to interferon treatment and viral double-stranded RNA, are necessary to activate RNase L. In contrast, unfolded proteins in the endoplasmic reticulum activate Ire1p, a transmembrane serine/threonine kinase and endoribonuclease. To probe their similarities and differences, molecular properties of wild-type and mutant forms of human RNase L and yeast Ire1p were compared. Surprisingly, RNase L and Ire1p showed mutually exclusive RNA substrate specificity and partially overlapping but not identical requirements for phylogenetically conserved amino acid residues in their nuclease domains. A functional model for RNase L was generated based on the comparative analysis with Ire1p that assigns novel roles for ankyrin repeats and kinase-like domains.

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Corresponding author
Reprint requests to: Robert H. Silverman, Department of Cancer Biology, NB40, The Lerner Research Institute, The Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, Ohio 44195, USA; e-mail: silverr@ccf.org.
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RNA
  • ISSN: 1355-8382
  • EISSN: 1469-9001
  • URL: /core/journals/rna
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