Biochemical characterization of the topoisomerase domain of Methanopyrus kandleri topoisomerase V.

ABSTRACT: Topoisomerases are ubiquitous enzymes that modify the topological state of DNA inside the cell and are essential for several cellular processes. Topoisomerase V is the sole member of the type IC topoisomerase subtype. The topoisomerase domain has a unique fold among topoisomerases, and the putative active site residues show a distinct arrangement. The present study was aimed at identifying the roles of the putative active site residues in the DNA cleavage/religation process. Residues Arg-131, Arg-144, His-200, Glu-215, Lys-218, and Tyr-226 were mutated individually to a series of conservative and non-conservative amino acids, and the DNA relaxation activity at different pH values, times, and enzyme concentrations was compared with wild-type activity. The results suggest that Arg-144 is ess

SUBMITTER: Rajan R 

PROVIDER: S-EPMC4200249 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature