Primer terminus stabilization at the phi 29 DNA polymerase active site. Mutational analysis of conserved motif KXY.

@article{Blasco1995PrimerTS,
  title={Primer terminus stabilization at the phi 29 DNA polymerase active site. Mutational analysis of conserved motif KXY.},
  author={Maria A Blasco and Juan Felipe M{\'e}ndez and Jose M. Lazaro and Luis Blanco and M. Salas},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 6},
  pages={2735-40}
}
phi 29 DNA polymerase shares with other DNA-dependent DNA polymerases several regions of amino acid homology along the primary structure. A conserved amino acid motif, located in the C-terminal portion of the polypeptide and characterized by the amino acid sequence KK(K/R)Y, is conserved in the group of eukaryotic-type DNA polymerases. In the subgroup of DNA polymerases that have a protein-priming mechanism, this motif is restricted to the sequence KXY, X never being a positively charged amino… CONTINUE READING

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