A Hybrid Protein kinase-RNase in an Interferon-Induced Pathway?

FEBS Lett. 1993 Nov 15;334(2):149-52. doi: 10.1016/0014-5793(93)81701-z.

Abstract

The sequence of RNase L has been re-examined by computer analysis. We propose a molecular architecture of RNase L, with an unusual combination, in one protein chain, of 9 ankyrin-like repeats, a functional active protein kinase and a C-terminal catalytic RNase similar to the yeast protein, IRE1. The protein kinase may be involved in a new signal transduction pathway which remains to be discovered.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ankyrins / chemistry
  • Consensus Sequence
  • Conserved Sequence
  • Databases, Factual
  • Endoribonucleases / biosynthesis*
  • Endoribonucleases / chemistry
  • Humans
  • Interferons / pharmacology*
  • Mice
  • Molecular Sequence Data
  • Protein Kinases / biosynthesis*
  • Protein Kinases / chemistry
  • Protein Multimerization
  • Sequence Homology, Amino Acid

Substances

  • Ankyrins
  • Interferons
  • Protein Kinases
  • Endoribonucleases
  • 2-5A-dependent ribonuclease