Literature DB >> 7523539

Fascination with 2-5A-dependent RNase: a unique enzyme that functions in interferon action.

R H Silverman1.   

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.

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Year:  1994        PMID: 7523539     DOI: 10.1089/jir.1994.14.101

Source DB:  PubMed          Journal:  J Interferon Res        ISSN: 0197-8357


  30 in total

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Review 4.  Making (anti)sense of non-coding sequence conservation.

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Authors:  J Martínez-Costas; C González-López; V N Vakharia; J Benavente
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Review 6.  Viral proteins that bind double-stranded RNA: countermeasures against host antiviral responses.

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Review 7.  Decoding the complexity of type I interferon to treat persistent viral infections.

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Review 8.  Interaction of hepatitis C virus with the type I interferon system.

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9.  Suppression of NYVAC Infection in HeLa Cells Requires RNase L but Is Independent of Protein Kinase R Activity.

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10.  Virus-host coevolution: common patterns of nucleotide motif usage in Flaviviridae and their hosts.

Authors:  Francisco P Lobo; Bruno E F Mota; Sérgio D J Pena; Vasco Azevedo; Andréa M Macedo; Andreas Tauch; Carlos R Machado; Glória R Franco
Journal:  PLoS One       Date:  2009-07-20       Impact factor: 3.240

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