Mammalian Genome

, Volume 11, Issue 11, pp 989–992

Analysis and origins of the human and mouse RNase L genes: mediators of interferon action

  • Aimin  Zhou
  • Huiqin  Nie
  • Robert H.  Silverman

DOI: 10.1007/s003350010194

Cite this article as:
Zhou, A., Nie, H. & Silverman, R. (2000) 11: 989. doi:10.1007/s003350010194

Abstract.

The 2′,5′-oligoadenylate-activated enzyme, RNase L, is an endoribonuclease implicated in the antiviral and apoptotic activities of interferons. To probe the genetics of the 2-5A system, the human and mouse genes were cloned, characterized, and compared. The first coding exon of both genes encodes the regulatory regions of RNase L, 67–70% of the proteins including nine ankyrin repeats, the 2-5A binding domain, and several protein kinase homology motifs. In contrast, the coding sequence for the ribonuclease domain in the mouse and human gene is divided among three exons. The transcriptional start site of the human RNase L gene was located in noncoding exon I by primer extension analysis. A complete coding sequence of mouse RNase L was obtained revealing a 735-amino acid protein with 64% identity to human RNase L. A hypothesis is presented concerning the evolutionary relationship of RNase L to both an ankyrin repeat protein kinase and the kinase-endoribonuclease, IRE1, that mediates the unfolded protein response.

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Copyright information

© Springer-Verlag New York Inc. 2000

Authors and Affiliations

  • Aimin  Zhou
    • 1
  • Huiqin  Nie
    • 1
  • Robert H.  Silverman
    • 1
  1. 1.Department of Cancer Biology, NB-40, Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, Ohio 44195, USAUS

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