The bipartite genome of red clover necrotic mosaic virus (RCNMV) was translated in nuclease-treated rabbit reticulocyte lysate with the synthesis of three principal translation products of molecular weights 39,000, 36,000, and 34,000. The 39,000 translation product was shown to be RCNMV coat protein by peptide mapping after partial proteolysis and by specific immunoprecipitation. RCNMV coat protein was shown to be coded for on the larger RNA (RNA-1) of the bipartite genome by hybrid-arrested translation using complementary DNA prepared to each of the fractionated RNAS. The 36,000-molecular weight product was also translated from RNA-1 while the 34,000-molecular weight product was not. Preliminary evidence indicated that the RCNMV coat protein is translated from a subgenomic species of RNA-1.