A hybrid protein kinase-RNase in an interferon-induced pathway?

FEBS letters ·Vol. 334 ·No. 2 ·1993-11-15 ·Pages 149-52

Bork P, Sander C

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.

MeSH Terms

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

Chemicals

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

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Bork P

EMBL, Heidelberg, Germany.

Sander C

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(93)81701-z

Published

1993-11-15

Pages

149-52

Language

English

Region

England

NLM ID

0155157

Subset

External Links

PubMed source DOI: 10.1016/0014-5793(93)81701-z View journal details

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A hybrid protein kinase-RNase in an interferon-induced pathway?

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