title: Fascination with 2-5A-dependent RNase: a unique enzyme that functions in interferon action.
abstract: Interferon (IFN) treatment of cells results in the induction of 2-5A-synthetases, double-stranded RNA-activated enzymes that produce unusual 5'-phosphorylated 2',5'-linked oligoadenylates known as 2-5A. 2.5A activates a unique IFN-induced endoribonuclease, the 2-5A-dependent RNase (RNase L), that is capable of degrading both viral and cellular RNA. The expression cloning of 2-5A-dependent RNase is leading to meaningful analysis of the physiological functions of the 2-5A system. For example, expression in mouse cells of a dominant-negative mutant form of 2-5A-dependent RNase suppressed both the antiencephalomyocarditis virus and anticellular activities of IFN. Future investigations into this intriguing ribonuclease pathway promise to provide an intricate view into a molecular pathway of IFN action.
authors.affiliation: Research Institute, Cleveland Clinic Foundation, OH 44122.
authors.forename: R H
authors.initials: RH
authors.lastname: Silverman
mesh_terms: D002874:Chromosome Mapping; D003001:Cloning, Molecular; D004722:Endoribonucleases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D006801:Humans; D007372:Interferons / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D007372:Interferons; D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease