[Construction of a dps mutant and its functional analysis in Deinococcus radiodurans].

Dps (DNA protection during starvation) is a member of the iron-binding protein family in prokaryotes. It has been shown previously that Dps possesses ferroxidase activity and the ability to sequester iron that seems to protect DNA from oxidative damage. Based on the method of Polymerase Chain Reaction and homologous genetic recombination in vivo, the gene (DRB0092) encoding a Dps protein homology in the extremely radioresistant bacterium Deinococcus radiodurans was deleted from the wild type strain R1 genome.

[Effects of PprI and RecX on antioxidant activity of Deinococcus radiodurans].

Effects of mutations of Pprl (Dr0167) and RecX (Dr1310), which are relative to radioresistance, on reactive oxygen species scavenging activities in Deinococcus radiodurans were investigated using gene mutation, chemiluminescence measurement and enzyme activity analysis. Their possible regulating functions on the activities of antioxidant enzymes was evaluated. Results show that mutant that lacks PprI is remarkably sensitive to reactive oxygen species and its enzyme activities of catalase and superoxide dismutase decrease significantly.

[Construction and functional analysis of the crtl gene disruptant in Deinococcus radiodurans].

With the method of Polymerase Chain Reaction and homologous genetic recombination in vivo, the key gene encoding bacterial-type phytoene desaturase (Crtl) which controls the carotenoids biosynthesis pathway in the non-photosynthetic and extremely radioresistant bacterium Deinococcus radiodurans was deleted from the genome. The colorless mutant obtained was designated as M61. Survival rates of mutant strain and wild type strain were investigated under different doses of gamma-radiation and hydrogen peroxide.