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Characterization of RecA424 and RecA670 proteins from ${it Deinococcus radiodurans}$

Sato, Katsuya; Narumi, Issei; Kikuchi, Masahiro; Kitayama, Shigeru; Yanagisawa, Tadashi*; Yamamoto, Kazuo; Watanabe, Hiroshi

RecA protein is considered to be the most important participant in the radiation resistance of ${it Deinococcus radiodurans}$. We identified a new ${it recA}$ mutation (${it recA424}$) in the DNA-repair deficient mutant strain KI696, the phenotype of which is remarkably different from mutant strain rec30 carrying ${it recA670}$. In vitro, neither RecA424 nor RecA670 could promote DNA strand exchange, indicating that both RecA424 and Rec670 are defective in recombination activity. RecA424 promoted the autocleavage reaction of LexA in vitro, whereas RecA670 did not. The LexA level in KI696 was decreased following $$gamma$$-irradiation. However, the LexA level in strain rec30 was constant irrespective of irradiation. These results indicate that RecA424 retains co-protease activity, whereas RecA670 does not. While strain rec30 is extremely radiation sensitive, strain KI696 is only slightly sensitive. Together, these observations suggest that the co-protease activity rather than the recombination activity of RecA contributes to the radiation resistance in ${it D. radiodurans}$.

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Category:Biochemistry & Molecular Biology

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