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National Institute for Medical Research, Mill Hill, London NW7 1AA, England
The fate of early virus messenger RNA in the cytoplasm of vaccinia-infected L cells has been studied during the first hour after infection. The RNA is made in the virus core structure from which it is rapidly released. It accumulates in the polyribosome fraction, where at least 75% is bound to ribosomes through an EDTA-sensitive link. Three distinct structures have been identified as possible intermediates in virus polyribosome formation. The first is a ribonucleoprotein complex (RNP) in which virus RNA is associated with cellular proteins. A complex having apparently similar properties, is formed when virus RNA is added to a cytoplasmic extract in vitro. The other two structures may consist of an RNP moiety associated with the small ribosomal subunit, or with a single ribosome. At least part of the RNA isolated as RNP appears to be a precursor of the virus messenger found in polyribosomes.
* Present address: Department of Microbiology, Rutgers Medical School, New Brunswick, New Jersey, U.S.A.
Present address: The Stefan S. Nicolau Institute of Virology, 285 Sos. Mihai Bravu, Bucharest, Romania.
Received 21 October 1974;
accepted 8 January 1975.
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