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Activation of interferon-regulated, dsRNA-dependent enzymes by human immunodeficiency virus-1 leader RNA.
SenGupta DN; Silverman RH; Department of Pathology, Uniformed Services
June 30, 1989
Nucleic Acids Res. 1989 Feb 11;17(3):969-78. Unique Identifier :

Human immunodeficiency virus-1 (HIV-1) leader RNA, which contains double-stranded regions due to inverted repeats, was shown to activate the dsRNA-dependent enzymes associated with the interferon system. HIV-1 leader RNA produced in vitro using SP6 RNA polymerase was characterized using probes for antisense and sense-strand RNA. The RNA preparation was free from significant levels of antisense RNA. HIV-1 leader RNA was shown to activate dsRNA-dependent protein kinase in a cell-free system from interferon-treated HeLa cells. Affinity resins, consisting of HIV-1 leader RNA covalently attached to cellulose, immobilized and activated dsRNA-dependent protein kinase and 2-5A-synthetase. HIV-1 leader RNA, therefore, may be a contributing factor in the mechanism by which interferon inhibits HIV replication.

Cell-Free System Enzyme Activation Enzymes, Immobilized Hela Cells Human HIV-1/*GENETICS Interferon Type I/*PHYSIOLOGY Plasmids Protein Kinases/METABOLISM Resins, Synthetic RNA, Double-Stranded/*PHYSIOLOGY RNA, Messenger/BIOSYNTHESIS/*PHYSIOLOGY Support, U.S. Gov't, Non-P.H.S. Support, U.S. Gov't, P.H.S. 2',5'-Oligoadenylate Synthetase JOURNAL ARTICLE