Nucleic acid binding properties of the 92-kDa replicase subunit of alfalfa mosaic virus produced in yeast.
The 92-kDa non-structural protein of alfalfa mosaic virus (one of the replicase subunits) was synthesized by Saccharomyces cerevisiae transformed with a recombinant expression vector. The yeast-expressed protein had the immunological and size characteristics of the naturally made viral protein. It was partially purified and its nucleic acid binding properties were tested by gel-retardation electrophoresis and nitrocellulose adsorption. The protein interacted with single-stranded RNA, double-stranded RNA and double-stranded DNA in a salt-dependent manner, with a slight preference for RNA. These properties may be related to its putative function as a core RNA polymerase.
Erny
C
C
Institut de Biologie Moléculaire des Plantes du C.N.R.S., Université Louis Pasteur, Strasbourg, France.
Schoumacher
F
F
Godefroy-Colburn
T
T
Stussi-Garaud
C
C
D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D000455:Medicago sativa / Q000382:microbiology*; D009029:Mosaic Viruses / Q000201:enzymology* / Q000235:genetics; D010957:Plasmids; D012367:RNA, Viral / Q000096:biosynthesis* / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014170:Transformation, Genetic; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism
D012367:RNA, Viral; D014764:Viral Proteins