A conserved 3′→5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases

@article{Bernad1989AC3,
  title={A conserved 3′→5′ exonuclease active site in prokaryotic and eukaryotic DNA polymerases},
  author={A. Bernad and L. Blanco and J. L{\'a}zaro and G. Mart{\'i}n and M. Salas},
  journal={Cell},
  year={1989},
  volume={59},
  pages={219-228}
}
The 3'----5' exonuclease active site of E. coli DNA polymerase I is predicted to be conserved for both prokaryotic and eukaryotic DNA polymerases based on amino acid sequence homology. Three amino acid regions containing the critical residues in the E. coli DNA polymerase I involved in metal binding, single-stranded DNA binding, and catalysis of the exonuclease reaction are located in the amino-terminal half and in the same linear arrangement in several prokaryotic and eukaryotic DNA… Expand
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  • B. Sanjanwala, A. Ganesan
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1989
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