S. Chamnongpol et al., ATYPICAL OXIDATIVE STRESS REGULATION OF A XANTHOMONAS-ORYZAE PV ORYZAE MONOFUNCTIONAL CATALASE, Canadian journal of microbiology, 41(6), 1995, pp. 541-547
Catalase is an important oxidative stress protective enzyme. We have s
hown in Xanthomonas oryzae pv. oryzae that catalase has atypical regul
ation in response to stresses and growth conditions. The superoxide ge
nerators paraquat and menadione at subinhibitory concentrations for gr
owth were potent inducers (8.3 and 10.4 fold, respectively) of the cat
alase of X. oryzae pv. oryzae. In contrast, H2O2 under all conditions
tested was a poor inducer of catalase. It gave a maximum induction lev
el of 2.4 fold, while ascorbate produced an intermediate level of indu
ction (4.5 fold). Unexpectedly, methyl methanesulphonate, a DNA methyl
ating agent and mutagen, was a potent inducer of catalase (8 fold). Ca
talase induction required de novo synthesis of the enzyme and aerobic
growth but it was independent of growth phase. Catalase induction by s
uperoxide generators and methyl methanesulphonate was due to increasin
g synthesis of the 80 000 Da monofunctional catalase. Similar patterns
of catalase induction by various agents were observed in all Xanthomo
nas strains tested, except that paraquat did not induce catalase in th
e strains with high paraquat resistance. The data illustrate novel asp
ects of catalase regulation in Xanthomonas strains that differ from th
at in other microbes. This may have important consequences for plant-m
icrobe interactions.