A hybrid protein kinase-RNase in an interferon-induced pathway?
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.
Bork
P
P
EMBL, Heidelberg, Germany.
Sander
C
C
D000595:Amino Acid Sequence; D000818:Animals; D017487:Ankyrins / Q000737:chemistry; D016384:Consensus Sequence; D017124:Conserved Sequence; D016208:Databases, Factual; D004722:Endoribonucleases / Q000096:biosynthesis* / Q000737:chemistry; D006801:Humans; D007372:Interferons / Q000494:pharmacology*; D051379:Mice; D008969:Molecular Sequence Data; D011494:Protein Kinases / Q000096:biosynthesis* / Q000737:chemistry; D055503:Protein Multimerization; D017386:Sequence Homology, Amino Acid
D017487:Ankyrins; D007372:Interferons; D011494:Protein Kinases; D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease