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Cloning and characterization of a RNAse L inhibitor. A new component of the interferon-regulated 2-5A pathway.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1995 Jun 02; Vol. 270 (22), pp. 13308-17. - Publication Year :
- 1995
-
Abstract
- The 2-5A/RNase L system is considered as a central pathway of interferon (IFN) action and could possibly play a more general physiological role as for instance in the regulation of RNA stability in mammalian cells. We describe here the expression cloning and initial characterization of RLI (for RNase L inhibitor), a new type of endoribonuclease inhibitor. RLI cDNA codes for a 68-kDa polypeptide whose expression is not regulated by IFN. Its expression in reticulocyte extracts antagonizes the 2-5A binding ability and the nuclease activity of endogenous RNase L or the cloned 2DR polypeptide. The inhibition requires the association of RLI with the nuclease and is dependent on the ratio between the two proteins. Likewise RLI is coimmunoprecipitated with the RNase L complex by a nuclease-specific antibody. RLI does not lead to 2-5A degradation or to irreversible modification of RNase L. The overexpression of RLI in stably transfected HeLa cells inhibits the antiviral activity of IFN on encephalomyocarditis virus but not on vesicular stomatitis virus. RLI therefore appears as the first described and potentially important mediator of the 2-5A/RNase L pathway.
- Subjects :
- Amino Acid Sequence
Base Sequence
Cell Line
Cloning, Molecular
DNA, Complementary
Endoribonucleases metabolism
Gene Expression Regulation
Humans
Interferons pharmacology
Molecular Sequence Data
Proteins metabolism
RNA, Messenger genetics
RNA, Messenger metabolism
ATP-Binding Cassette Transporters
Adenine Nucleotides metabolism
Chaperonins
Endoribonucleases antagonists & inhibitors
Oligoribonucleotides metabolism
Proteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 270
- Issue :
- 22
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 7539425
- Full Text :
- https://doi.org/10.1074/jbc.270.22.13308