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J Virol. 1970 July; 6(1): 1-11
Copyright © 1970 American Society for Microbiology. All Rights Reserved.

Transcription In Vitro by Reovirus-Associated Ribonucleic Acid-Dependent Polymerase ¹

Roche Institute of Molecular Biology, Nutley, New Jersey 07110

ABSTRACT

Digestion of purified reovirus type 3 with chymotrypsin degrades 70% of the viral protein and converts the virions to subviral particles (SVP). The SVP contain 3 of the 6 viral structural proteins and all 10 double-stranded ribonucleic acid (RNA) genome segments but not adenine-rich, single-stranded RNA. An RNA polymerase which is structurally associated with SVP transcribes one strand of each genome segment by a conservative mechanism in vitro. The single-stranded products include large (1.2 x 10⁶ daltons), medium (0.7 x 10⁶ daltons), and small (0.4 x 10⁶ daltons) molecules which hybridize exclusively with the corresponding genome segments. The enzyme obtained by heating virions at 60 C synthesizes similar products. Kinetic and pulse-chase studies indicate that the different-sized products are synthesized simultaneously but at rates which are in the order: small > medium > large.

¹ This work was reported in part at the meeting of the Federated American Societies of Experimental Biology, April 1970.

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