Effect of Rauscher leukemia virus-specific proteins on reverse transcriptase. Binding between reverse transcriptase and p30.
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.
D007118:Immunoassay; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D012194:RNA-Directed DNA Polymerase / Q000302:isolation & purification / Q000378:metabolism*; D011925:Rauscher Virus / Q000201:enzymology*; D014764:Viral Proteins / Q000302:isolation & purification / Q000502:physiology
D046911:Macromolecular Substances; D014764:Viral Proteins; D012194:RNA-Directed DNA Polymerase