131 research outputs found
Selected reactive oxygen species and antioxidant enzymes in common bean after Pseudomonas syringae pv. phaseolicola and Botrytis cinerea infection
Phaseolus vulgaris cv. Korona plants were
inoculated with the bacteria Pseudomonas syringae pv.
phaseolicola (Psp), necrotrophic fungus Botrytis cinerea
(Bc) or with both pathogens sequentially. The aim of the
experiment was to determine how plants cope with multiple
infection with pathogens having different attack strategy.
Possible suppression of the non-specific infection with
the necrotrophic fungus Bc by earlier Psp inoculation was
examined. Concentration of reactive oxygen species
(ROS), such as superoxide anion (O2
-) and H2O2 and
activities of antioxidant enzymes such as superoxide dismutase
(SOD), catalase (CAT) and peroxidase (POD) were
determined 6, 12, 24 and 48 h after inoculation. The
measurements were done for ROS cytosolic fraction and
enzymatic cytosolic or apoplastic fraction. Infection with
Psp caused significant increase in ROS levels since the
beginning of experiment. Activity of the apoplastic
enzymes also increased remarkably at the beginning of
experiment in contrast to the cytosolic ones. Cytosolic
SOD and guaiacol peroxidase (GPOD) activities achieved
the maximum values 48 h after treatment. Additional forms
of the examined enzymes after specific Psp infection were
identified; however, they were not present after single Bc
inoculation. Subsequent Bc infection resulted only in
changes of H2O2 and SOD that occurred to be especially
important during plant–pathogen interaction. Cultivar Korona
of common bean is considered to be resistant to Psp and mobilises its system upon infection with these bacteria.
We put forward a hypothesis that the extent of defence
reaction was so great that subsequent infection did not
trigger significant additional response
Effect of the distal histidine on the peroxidatic activity of monomeric cytoglobin
The reaction of hydrogen peroxide with ferric human cytoglobin and a number of distal histidine variants were studied. The peroxidase activity of the monomeric wildtype protein with an internal disulfide bond, likely to be the form of the protein in vivo, exhibits a high peroxidase-like activity above that of other globins such as myoglobin. Furthermore, the peroxidatic activity of wildtype cytoglobin shows increased resistance to radical-based degradation compared to myoglobin. The ferryl form of wildtype cytoglobin is unstable, but is able to readily oxidize substrates such as guaiacol. In contrast distal histidine mutants of cytoglobin (H81Y and H81V) show very low peroxidase activity but enhanced radical-induced degradation. Therefore, the weakly bound distal histidine appears to modulate ferryl stability and limit haem degradation. These data are consistent with a role of a peroxidase activity of cytoglobin in cell stress response mechanisms.</ns4:p
Acid invertase confers heat tolerance in rice plants by maintaining energy homoeostasis of spikelets
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