ABSTRACT
The purified p12 phosphoprotein of Rauscher murine leukemia virus was fractionated by ion exchange chromatography into subpopulations of molecules containing different amounts of covalently linked phosphate. Of the various phosphorylated forms of p12 protein purified from virions, only a species containing relatively little phosphate can bind in vitro to purified homologous 70S viral RNA. Using ultraviolet irradiation to stabilize ribonucleoprotein complexes in intact virions, the same molecular species of p12 phosphoprotein can be isolated in close association with the 70S viral genome. The results show that phosphorylation of type C viral p12 proteins influences the extent, but not the specificity, of their interaction with homologous viral RNA.
Subject(s)
Phosphates/metabolism , Phosphoproteins/metabolism , RNA, Viral/metabolism , Rauscher Virus/metabolism , Viral Proteins/metabolism , Rauscher Virus/radiation effects , Ultraviolet RaysABSTRACT
The stability of Rauscher leukemia virus (RLV) was investigated under certain laboratory conditions. The half life of the virus at 37 degrees was 7 hr, and considerably longer at lower temperatures. RNA dependent DNA polymerase activity was more stable than infectivity at all temperatures. Air dried virus had a half life of approximately 1 hr, but was rapidly inactivated by uv light or 70% alcohol.
