Analysis of the protein composition of alfalfa mosaic virus RNA-dependent RNA polymerase.
RNA-dependent RNA polymerase (RdRp) was solubilized and purified from cellular membranes isolated from alfalfa mosaic virus (AIMV)-infected tobacco by employing a procedure recently described for brome mosaic virus RdRp [R. Quadt and E.M.J. Jaspars, 1990, Virology 178, 189-194]. The purified AIMV RdRp is completely dependent on added template RNAs and exhibits a high degree of template specificity. Analysis of the protein composition of AIMV RdRp showed that AIMV-encoded proteins P1 and P2 and the coat protein (CP) are present in the active enzyme complex. Minus-strand synthesis by the AIMV RdRp is inhibited by AIMV CP. Native double-stranded AIMV RNAs are utilized as template for viral RNA synthesis by AIMV RdRp indicating that a helicase activity is present in the purified AIMV RdRp preparation.
Quadt
R
R
Department of Biochemistry, Gorlaeus Laboratories, Leiden University, The Netherlands.
Rosdorff
H J
HJ
Hunt
T W
TW
Jaspars
E M
EM
D015153:Blotting, Western; D002213:Capsid / Q000378:metabolism; D046911:Macromolecular Substances; D000455:Medicago sativa; D008970:Molecular Weight; D009029:Mosaic Viruses / Q000201:enzymology* / Q000254:growth & development; D012367:RNA, Viral / Q000096:biosynthesis; D012324:RNA-Dependent RNA Polymerase / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D013379:Substrate Specificity; D013698:Templates, Genetic; D014764:Viral Proteins / Q000378:metabolism
D046911:Macromolecular Substances; D012367:RNA, Viral; D014764:Viral Proteins; D012324:RNA-Dependent RNA Polymerase