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

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.

Extracted Key Phrases

9 Figures and Tables

02040'04'06'08'10'12'14'16
Citations per Year

178 Citations

Semantic Scholar estimates that this publication has 178 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Dong2001BasisFR, title={Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p.}, author={B Z Dong and Maho Niwa and Peter Walter and Robert Silverman}, journal={RNA}, year={2001}, volume={7 3}, pages={361-73} }