Translation of potato virus S RNA in vitro: evidence of protein processing.
RNA from potato virus S (PVS), a member of the carlavirus group, was translated in vitro in rabbit reticulocyte lysate. Time-course experiments revealed the largest product of Mr 190 kD, decreasing in intensity after 60-min incubations, correlating with the accumulation of a 150-kD peptide. This apparent processing could be blocked by the addition of the amino-acid analogues p-fluorophenylalanine and L-canavanine for phenylalanine and arginine, respectively. L-canavanine also appeared to specifically reduce the quantity of PVS (34 kD) coat protein, concomitant with the synthesis of a 36-kD peptide. Sucrose gradient-fractionated genomic RNA directed the synthesis of predominantly 190-kD peptides that appeared not to be processed in the absence of small molecular weight (subgenomic) RNA products.
Foster
G D
GD
University of Leicester, Department of Botany, UK.
Mills
P R
PR
D000524:Alphavirus / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D002213:Capsid / Q000235:genetics* / Q000378:metabolism; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010942:Plant Viruses / Q000235:genetics*; D011499:Protein Processing, Post-Translational; D011817:Rabbits; D012689:Sequence Homology, Nucleic Acid; D011198:Solanum tuberosum / Q000235:genetics* / Q000382:microbiology