BIOCHEMICAL CHARACTERIZATION OF XTHA AP-ENDONUCLEASE FROM HELICOBACTER PYLORI
Main Article Content
Authors
A.M. Turgimbaeva
National Center for Biotechnology, 13/5, Korgalzhyn road, Astana, 010000, Kazakhstan
L.N. Gumilyov Eurasian National University, Satpayev Street, 2, Astana, 010000, Kazakhstan
S.K. Abeldenov
National Center for Biotechnology, 13/5, Korgalzhyn road, Astana, 010000, Kazakhstan
M.K. Saparbayev
Institute of Gustav Roussy, CNRS UMR 8200, 114 Rue Edouard Vaillant, Villejuif, 94805, France
Y.M. Ramankulov
National Center for Biotechnology, 13/5, Korgalzhyn road, Astana, 010000, Kazakhstan
B.B. Khassenov
National Center for Biotechnology, 13/5, Korgalzhyn road, Astana, 010000, Kazakhstan
Abstract
About 50% of world population is infected by pathogenic bacterium Helicobacter pylori. During persistence in the human body, this microorganism encounters negative effects of reactive oxygen and nitrogen species (ROS, RNS) generated by neutrophils and macrophages, which damage bacterial DNA. Consequently, microorganism triggers a mechanism for eliminating DNA damages that is carried out by DNA repair enzymes. Base excision repair (BER) is one of the ways of DNA repair to eliminate oxidized, deaminated and alkylated nitrogenous bases. The key enzymes of BER are apurinic/apyrimidinic endonucleases (AP-endonucleases).
In this article research results of DNA repair activity of XthA AP-endonuclease from H. pylori (HpXthA) are presented. The optimal reaction conditions were determined for verifying the repair activity of HpXthA in vitro: low ionic strength, high concentration of Mg2+, pH 7-8 and 30°C incubation temperature. Kinetic parameters of AP-endonuclease, 3¢-phosphodiesterase and 3¢-phosphatase activity of HpXthA have been determined (kcat/KM = 1240, 44 and 5.4 µM-1·min-1, respectively).
Keywords
base excision repair, Helicobacter pylori, AP-endonuclease, AP-site, oxidative stress, oxidized DNA damage
Article Details
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