Effect of Rauscher leukemia virus-specific proteins on reverse transcriptase. Binding between reverse transcriptase and p30.

Abstract

The reverse transcriptase was purified to homogeneity from Rauscher leukemia virus by sequential column chromatography on phosphocellulose and DNA-cellulose. The purified enzyme, a single polypeptide chain with a molecular weight of approximately 70,000, interacts with major internal protein p30 of the same virus. The reverse transcriptase - p30 complex stimulated [3H]TMP incorporation into (dT)12 - (rA)n 2- to 3-fold compared to that observed with the purified enzyme alone. Monospecific antiserum made against either p30 or reverse transcriptase precipitated the entire complex. The sedimentation rate of the reverse transcriptase - p30 complex is approximately 12 S as estimated by glycerol gradient centrifugation, and the molecular weight is approximately 400,000 by chromatography on a Sepharose 6B column. The complex dissociates into its original components when treated with 0.8 M KCl.