In addition, high expression of katA from the pKatA plasmid (pBBR1MCS containing a full-length katA) selleck compound in the katA mutant (katA/pKatA) and the katA katG double mutant (katA katG/pKatA), in which the total catalase activity was extremely high (823 ± 57 and 809 ± 41 U mg−1 protein,

respectively), rendered the bacteria more tolerant to heat shock than the wild-type strain (Fig. 1). In X. campestris pv. campestris, the expressions of katA and katG are under the regulation of OxyR, a regulator of the genes involved in adaptive or cross-protection against H2O2 killing in Xanthomonas (Chauvatcharin et al., 2005; Mongkolsuk et al., 1998). The viability of X. campestris pv. campestris was measured in the absence or presence of OxyR to determine whether the regulator is required for heat shock tolerance. The oxyR mutant (Jittawuttipoka et al., 2009) was over 400-fold more sensitive to the heat treatment for 10 min than its parental strain (Fig. 1). The phenotypic change of the oxyR mutant Trametinib order was fully restored to the wild-type level when the mutant was complemented with pOxyR (an expression vector containing a full-length oxyR; (Jittawuttipoka et al., 2009) (Fig. 1). The oxyR mutant had a level of total catalase activity similar to that of the katA mutant (2.1 ± 0.5 and 1.2 ± 0.3 U mg−1 protein, respectively), but the former mutant was more sensitive

to the heat treatment than the latter mutant (400- and 100-fold, respectively). This was likely due to the inability of the oxyR mutant to upregulate both katA and katG, while in the katA mutant, katG could be upregulated by the stress. The heat-treatment survival of the oxyR mutant showed a correlation with the total catalase activity. The data show clearly that OxyR plays a protective role against heat mortality of X. campestris pv. campestris, probably through its function as a peroxide sensor and transcription regulator that controls the expression of katA and katG in response to the H2O2 generated

from the heat treatment. Alkyl hydroperoxide reductase (AhpC) plays a major role in the degradation of physiologically generated H2O2 in bacteria (Seaver & Imlay, 2001). The gene is also a member of the OxyR regulon. The contribution of ahpC to heat resistance Branched chain aminotransferase was evaluated using the ahpC mutant (Patikarnmonthon et al., 2010). After the heat treatment, the mutant showed resistance levels similar to those of the wild-type strain. This feature was unexpected, because other peroxide-protective mutants (katA, katG, and oxyR) were less resistant to the heat treatment than the wild-type strain. The lack of alteration in resistance to heat shock of the ahpC mutant was likely due to the OxyR-dependent increased expression of katA and katG that compensated for the inactivation of ahpC (Mongkolsuk et al., 2000; Charoenlap et al., 2005; Jittawuttipoka et al., 2009).