Mutational analysis of endonuclease V from Thermotoga maritima.

  title={Mutational analysis of endonuclease V from Thermotoga maritima.},
  author={Jianmin Huang and Jing Hua Lu and Francis Barany and Weiguo Cao},
  volume={41 26},
Endonuclease V nicks damaged DNA at the second phosphodiester bond 3' to inosine, uracil, mismatched bases, or abasic (AP) sites. Alanine scanning mutagenesis was performed in nine conserved positions of Thermotoga maritima endonuclease V to identify amino acid residues involved in recognition or endonucleolytic cleavage of these diverse substrates. Alanine substitution at D43, E89, and D110 either abolishes or substantially reduces inosine cleavage activity. These three mutants gain binding… CONTINUE READING

From This Paper

Topics from this paper.


Publications citing this paper.
Showing 1-10 of 11 extracted citations

Structural basis for incision at deaminated adenines in DNA and RNA by endonuclease V.

Progress in biophysics and molecular biology • 2015
View 3 Excerpts
Highly Influenced

Endonuclease V: an unusual enzyme for repair of DNA deamination

Cellular and Molecular Life Sciences • 2012
View 2 Excerpts

Similar Papers

Loading similar papers…