The VPg of tobacco etch virus RNA is the 49-kDa proteinase or the N-terminal 24-kDa part of the proteinase.
Preparations of tobacco etch virus (TEV) RNA which were purified by sucrose gradient centrifugation, digested with RNase, and analyzed by SDS-polyacrylamide gel electrophoresis contained proteins of 49, 32, and 24 kDa. The 49- and 24-kDa proteins reacted with polyclonal antiserum to the TEV 49-kDa proteinase while the 32-kDa protein reacted with anti-TEV serum. Further purification of the RNA by centrifugation through CsCl removed the coat protein (32 kDa), but not the 49- and 24-kDa proteins. The 49- and 24-kDa proteins did not migrate into a polyacrylamdie gel when the RNA was not digested with RNase. These results indicate that the VPg of TEV is either the 49-kDa proteinase or the 24 kDa that represents the amino-terminal half thereof.
Murphy
J F
JF
Department of Plant Pathology, University of Kentucky, Lexington 40546.
Rhoads
R E
RE
Hunt
A G
AG
Shaw
J G
JG
D002499:Centrifugation, Density Gradient; D010450:Endopeptidases / Q000235:genetics*; D010942:Plant Viruses / Q000235:genetics*; D012367:RNA, Viral / Q000032:analysis*; D014764:Viral Proteins / Q000235:genetics*
D012367:RNA, Viral; D014764:Viral Proteins; D010450:Endopeptidases