The vesicular stomatitis virus L protein possesses the mRNA methyltransferase activities.

We have previously shown that the vesicular stomatitis virus (VSV) host range mutant, hr 1, is completely defective for the mRNA methyltransferase activities, but can synthesize full-length, unmethylated mRNAs in vitro [S. M. Horikami and S. A. Moyer (1982). Proc. Natl. Acad. Sci. USA 79, 7694-7698] and in vivo [S. M. Horikami, F. De Ferra, and S. A. Moyer (1984). Virology 138, 1-15]. Here we have used the hr 1 mutant to identify the viral protein which possesses the methyltransferase activities. The wild-type VSV L and NS proteins, subunits of the viral RNA polymerase, were separately purified and added to high salt dissociated mutant hr 1 nucleocapsids for in vitro transcription reactions. The results show that the purified wild-type L protein, but not the NS protein, restores methylation and thus possesses the viral mRNA methyltransferase activities.