Biochemical and immunological properties of the reverse transcriptase associated with a hamster retrovirus.
Several properties of an RNA-directed DNA polymerase associated with a hamster retrovirus (HaRV) were examined and found to be similar to other polymerases from mammalian type-C viruses in that the enzyme (i) is more active with Mn2+ than Mg2+, (ii) uses the reverse transcriptase-specific poly(rCm).oligo(dG) template, (iii) possesses substantial endogenous polymerase activity and (iv) is strongly inhibited by homologous antisera and moderately inhibited by antisera directed against other type-C viruses. In contrast to previous reports of polymerases from other hamster viruses, HaRV polymerase is active in endogenous assays and the activity is associated with a 70,000 mol. wt. polypeptide in highly purified virions and with 70,000 and 85,000 mol. wt. polypeptides in fresh, unpurified virus. Only one major peak of polymerase activity eluted from DEAE-cellulose while subsequent elution of this peak from phosphocellulose produced two major peaks of polymerase activity. The mol. wt. of these two peaks were 70,000 and 85,000 by glycerol density-gradient sedimentation. The HaRV reverse transcriptase and p30 were found to be most closely related antigenically to other rodent retrovirus proteins.
D000818:Animals; D006224:Cricetinae; D000939:Epitopes; D008274:Magnesium / Q000378:metabolism; D008345:Manganese / Q000378:metabolism; D011119:Polynucleotides / Q000378:metabolism; D012194:RNA-Directed DNA Polymerase / Q000276:immunology / Q000378:metabolism*; D012190:Retroviridae / Q000201:enzymology*; D012260:Ribonucleases / Q000378:metabolism; D013698:Templates, Genetic
D000939:Epitopes; D011119:Polynucleotides; D008345:Manganese; D012194:RNA-Directed DNA Polymerase; D012260:Ribonucleases; D008274:Magnesium