NR AKMI
AU Scheffer,U.; Okamoto,T.; Forrest,J.M.S.; Rytik,P.G.; Müller,W.E.G.; Schröder,H.C.
TI Interaction of 68-kDa TAR RNA-binding protein and other cellular proteins with prion protein-RNA stem-loop
QU Journal of Neurovirology 1995 Dec; 1(5-6): 391-8
PT journal article
AB The RNA stem-loop structure of the trans-activating region TAR sequence of human immunodeficiency virus-1 mRNA is the binding site for a number of host cell proteins. A virtually identical set of proteins from HeLa nuclear extracts was found to bind to the predicted RNA hairpin element of prion protein (PrP) mRNA, as demonstrated in UV cross-linking/RNase protection and Northwestern assays. We show that the cellular TAR loop-binding protein, p68, is among those proteins which associate with PrP RNA. Competition experiments with various TAR RNA mutants revealed that binding of partially purified p68 to PrP RNA stem-loop occurs sequence-specifically. The 100-kDa 2-5A synthetase which is involved in the cellular antiviral defense was able to bind to PrP mRNA stem-loop in Northwestern blots with cytosolic proteins from HeLa cells treated with interferon. However, the PrP RNA failed to activate this enzyme in vitro, in contrast to TAR RNA.
IN An das hairpin Element der Prionprotein-mRNA binden die gleichen zellulären Proteine, wie an die RNA-stem-loop-structure der transaktivierenden Region TAR des HIV-1-Virus-1. Dazu gehört das zelluläre TAR-loop-bindende Protein p68. In Northwestern Blots mit zytosolischen Proteinen aus mit Interferon behandelten HeLa-Zellen bindet an den PrP mRNA stem-loop auch die 100-kDa 2-5A Synthetase, welche an der zellulären antiviralen Verteidigung beteiligt ist. Im Gegensatz zur TAR-RNA aktiviert aber die PrP-RNA dieses Enzym in vitro nicht.
ZR 35
MH 2',5'-Oligoadenylate Synthetase/metabolism; Base Sequence; Binding, Competitive/genetics; Blotting, Northern; Blotting, Western; HIV Long Terminal Repeat/*genetics; Hela Cells; Human; Lymphocytes/chemistry/enzymology/microbiology; Molecular Sequence Data; Mutagenesis/physiology; Nucleic Acid Conformation; Prions/*chemistry/*genetics/metabolism; RNA-Binding Proteins/metabolism; Receptors, Cell Surface/*metabolism; Support, Non-U.S. Gov't
AD Institut für Physiologische Chemie, Universität, Mainz, Germany.
SP englisch
PO England