Uniquely altered DNA replication fidelity conferred by an amino acid change in the nucleotide binding pocket of human immunodeficiency virus type 1 reverse transcriptase.

@article{Lewis1999UniquelyAD,
  title={Uniquely altered DNA replication fidelity conferred by an amino acid change in the nucleotide binding pocket of human immunodeficiency virus type 1 reverse transcriptase.},
  author={Dale E. A. Lewis and Katarzyna Bębenek and William A. Beard and Samuel H. Wilson and T. A. Kunkel},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 46},
  pages={32924-30}
}
Arginine 72 in human immunodeficiency virus type 1 reverse transcriptase (RT), a highly conserved residue among retroviral polymerases and telomerases, forms part of the binding pocket for the nascent base pair. We show here that replacement of Arg(72) by alanine strongly alters fidelity in a highly unusual manner. R72A reverse transcriptase is a frameshift and base substitution antimutator polymerase whose increased fidelity results both from increased nucleotide selectivity and from a… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 19 extracted citations

Similar Papers

Loading similar papers…