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. (C) 1998 Elsevier Science B.V.
cDNA cloning and expression analysis of the murine ribonuclease L inhibitor
De Coignac, A. B.; Bisbal, C.; Lebleu, B.; Salehzada, T.
1998-03-16 / vol 209 / pages 149-156
expression; pathway; gene; cells; 2-5a; cleavage; endonuclease; 2-5a system; intact; interferon; nucleotide sequence; pattern; rnase l; rnase-l inhibitor