Reconstitution in vitro of RNase H activity by using purified N-terminal and C-terminal domains of human immunodeficiency virus type 1 reverse transcriptase.

@article{Hostomsky1991ReconstitutionIV,
  title={Reconstitution in vitro of RNase H activity by using purified N-terminal and C-terminal domains of human immunodeficiency virus type 1 reverse transcriptase.},
  author={Zdenek Hostomsky and Zuzana Hostomska and Gracia Hudson and Ellen W Moomaw and Beverly R. Nodes},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1991},
  volume={88 4},
  pages={
          1148-52
        }
}
Two constituent protein domains of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase were expressed separately and purified to homogeneity. The N-terminal domain (p51) behaves as a monomeric protein exhibiting salt-sensitive DNA polymerase activity. The C-terminal domain (p15) on its own has no detectable RNase H activity. However, the combination of both isolated p51 and p15 in vitro leads to reconstitution of RNase H activity on a defined substrate. These results demonstrate… CONTINUE READING
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