Site-specific mutagenesis of conserved residues within Walker A and B sequences of Escherichia coli UvrA protein.

@article{Myles1991SitespecificMO,
  title={Site-specific mutagenesis of conserved residues within Walker A and B sequences of Escherichia coli UvrA protein.},
  author={G M Myles and J. E. Hearst and Aziz Sancar},
  journal={Biochemistry},
  year={1991},
  volume={30 16},
  pages={3824-34}
}
UvrA is the ATPase subunit of the DNA repair enzyme (A)BC excinuclease. The amino acid sequence of this protein has revealed, in addition to two zinc fingers, three pairs of nucleotide binding motifs each consisting of a Walker A and B sequence. We have conducted site-specific mutagenesis, ATPase kinetic analyses, and nucleotide binding equilibrium measurements to correlate these sequence motifs with activity. Replacement of the invariant Lys by Ala in the putative A sequences indicated that… CONTINUE READING

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