cDNA cloning and expression analysis of the murine ribonuclease L inhibitor

Benoit De Coignac, A.; Bisbal, C.; Lebleu, B.; Salehzada, T.


1998-03-16 / vol 209 / pages 149-56


The 2-5A/RNase L system is one of the pathways induced by interferon (IFN). It plays a major role in the antiviral and antiproliferative activities of IFNs. Recently, we have shown that the activity of the RNase L could be inhibited by a proteic inhibitor, the RNase L Inhibitor (RLI). Human RLI (Hu-RLI) was cloned and characterized. We describe here the isolation and characterization of the cDNA encoding the murine RLI (Mu-RLI). Hu-RLI and Mu-RLI protein have 98% amino acid identity. Mu-RLI is functionally homologous to Hu-RLI, and all the structural features and amino acid sequence motifs of Hu-RLI are conserved in Mu-RLI. Moreover, reticulocyte lysate translated Mu-RLI protein is also able to inhibit 2-5A binding on 2-5A-dependent RNAse-L. Northern blot analysis revealed that Mu-RLI cDNA hybridizes with one mRNA of 3.5 kb except for the testis where two mRNA of 3.5 and 2.1 kb, respectively, are detected, suggesting a tissue-specific regulation.

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Humans; Animals; Mice; Male; Amino Acid Sequence; Molecular Sequence Data; Base Sequence; Transcription, Genetic; Sequence Alignment; Sequence Homology, Amino Acid; *Protein Biosynthesis; Binding, Competitive; Cloning, Molecular; DNA, Complementary; Conserved Sequence; Saccharomyces cerevisiae/genetics; *ATP-Binding Cassette Transporters; *Chaperonins; Organ Specificity; Adenine Nucleotides/metabolism; Oligoribonucleotides/metabolism; Enzyme Inhibitors/*chemistry/pharmacology; Methanococcus/genetics; Proteins/*chemistry/pharmacology; Recombinant Proteins/biosynthesis/chemistry/pharmacology

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