Some amino acids of the Pseudomonas aeruginosa MutL D(Q/M)HA(X)(2)E(X)(4)E conserved motif are essential for the in vivo function of the protein but not for the in vitro endonuclease activity.

@article{Correa2011SomeAA,
  title={Some amino acids of the Pseudomonas aeruginosa MutL D(Q/M)HA(X)(2)E(X)(4)E conserved motif are essential for the in vivo function of the protein but not for the in vitro endonuclease activity.},
  author={Elisa M. E. Correa and Mariana A. Martina and L A Luis A de Tullio and Carlos Enrique Argara{\~n}a and Jos{\'e} Luis Barra},
  journal={DNA repair},
  year={2011},
  volume={10 11},
  pages={1106-13}
}
Human and Saccharomyces cerevisiae MutLα, and some bacterial MutL proteins, possess a metal ion-dependent endonuclease activity which is important for the in vivo function of these proteins. Conserved amino acids of the C-terminal region of human PMS2, S. cerevisiae PMS1 and of some bacterial MutL proteins have been implicated in the metal-binding/endonuclease activity. However, the contribution of individual amino acids to these activities has not yet been fully elucidated. In this work we… CONTINUE READING

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