Is Catalase Activity One of the Factors Associated with Maize Resistance to Aspergillus flavus?

Plant responses to biotic and abiotic stresses are usually accompanied by the release of reactive oxygen species including hydrogen peroxide. Hydrogen peroxide plays a direct role in defense and is involved in many signal transduction pathways that lead to the proliferation of other defenses. Because catalase helps to maintain reactive oxygen homeostasis during biotic and abiotic stress, its activity was measured in various cob tissues during maize ear development. Catalase activity was determined in immature and mature embryos, pericarp, and rachis tissues of maize lines that are resistant and susceptible to Aspergillus flavus infection. The effect of fungal inoculation on catalase activity was also measured. Over two years of field experimentation, a correlation was observed between resistance and the level of catalase-specific activity in immature embryos, which was significantly higher in resistant lines (P < 0.0001). Furthermore, catalase activity in the resistant lines was significantly higher in immature embryos from inoculated ears (P = 0.0199). No correlation was observed between resistance and catalase activity in other ear tissues. Levels of hydrogen peroxide, the catalase substrate, and salicylic acid in the embryo were also determined. The resistant lines showed lower levels of H2O2 (P < 0.0001) and higher levels of salicylic acid (P < 0.0001) as compared with the susceptible lines. Catalase 3 was sequenced from the aflatoxin-resistant (Mp313E) and -susceptible (SC212m) inbreds. The predicted amino acid sequence indicated that there was a 20-aa deletion in the resistant inbred that might affect enzymatic activity. Unlike many plant-pathogen interactions, it appears that lowering H2O2 levels helps to prevent A. flavus infection and subsequent aflatoxin accumulation.

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Catalase activity and the survival of Pseudomonas putida, a root colonizer, upon treatment with peracetic acid

Canadian Journal of Microbiology ◽

10.1139/w01-002 ◽

2001 ◽

Vol 47 (3) ◽

pp. 222-228 ◽

Cited By ~ 6

Author(s):

Anne J Anderson ◽

Charles D Miller

Keyword(s):

Hydrogen Peroxide ◽

Pseudomonas Putida ◽

Peracetic Acid ◽

Catalase Activity ◽

Specific Activity ◽

Active Oxygen Species ◽

Oxygen Species ◽

Deficient Mutant ◽

Wild Type ◽

Cell Extracts

Peracetic acid is used as a sterilant in several industrial settings. Cells of a plant-colonizing bacterium, Pseudomonas putida in liquid suspension, were more sensitive to killing by peracetic acid when they lacked a major catalase activity, catalase A. Low doses of peracetic acid induced promoter activity of the gene encoding catalase A and increased total catalase specific activity in cell extracts. Microbes present in native agricultural soils rapidly degraded the active oxygen species present in peracetic acid. The simultaneous release of oxygen was consistent with a role for catalase in degrading the hydrogen peroxide that is part of the peracetic acid-equilibrium mixture. Amendment of sterilized soils with wild-type P. putida restored the rate of degradation of peracetic acid to a higher level than was observed in the soils amended with the catalase A-deficient mutant. The association of the bacteria with the plant roots resulted in protection of the wild-type as well as the catalase-deficient mutant from killing by peracetic acid. No differential recovery of the wild-type and catalase A mutant of P. putida was observed from roots after the growth matrix containing the plants was flushed with peracetic acid.Key words: Pseudomonas putida (Pp), activated oxygen species (AOS), hydrogen peroxide, luciferase, colonization.

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In vivo generation of hydrogen peroxide by rat kidney cortex and glomeruli

AJP Renal Physiology ◽

10.1152/ajprenal.1989.256.1.f158 ◽

1989 ◽

Vol 256 (1) ◽

pp. F158-F164 ◽

Cited By ~ 6

Author(s):

B. R. Guidet ◽

S. V. Shah

Keyword(s):

Hydrogen Peroxide ◽

Catalase Activity ◽

Renal Cortex ◽

Specific Activity ◽

Rat Kidney ◽

Kidney Cortex ◽

Compound I ◽

Rat Kidney Cortex ◽

Hydrogen Peroxide Generation

The purpose of this study was to demonstrate in vivo generation of hydrogen peroxide by rat renal cortex and glomeruli. Aminotriazole irreversibly inactivates catalase only in the presence of hydrogen peroxide, and previous studies have shown that aminotriazole-mediated inhibition of catalase is a measure of in vivo changes in the hydrogen peroxide generation. Aminotriazole injected intraperitoneally caused a dose-dependent (0.1-1 g/kg) and a time-dependent (15, 30, 60, 90, 120 min) inhibition of the catalase activity in renal cortex. We confirmed that catalase inactivation by aminotriazole was due to formation of a catalase-hydrogen peroxide intermediate (compound I) because catalase inactivation was prevented by ethanol (2 g/kg), a competitive substrate for compound I. The specific activity of catalase in the glomeruli [0.27 +/- 0.026 k/mg protein (where k is the first-order reaction rate constant), n = 5] was significantly lower than the specific activity in the tubules (1.04 +/- 0.15 k/mg protein, n = 5) obtained from the same rats. The residual catalase activity (RCA) in the glomeruli (0.05 +/- 0.01 k/mg protein) was 19% of control values at 90 min after aminotriazole injection (1 g/kg). Taken together these data provide evidence for in vivo generation of hydrogen peroxide by rat renal cortex and glomeruli under normal conditions. Aminotriazole-mediated inhibition of catalase has been used in previous studies as a measure of in vivo changes in the hydrogen peroxide generation.(ABSTRACT TRUNCATED AT 250 WORDS)

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The Periplasmic, Group III Catalase of Vibrio fischeriIs Required for Normal Symbiotic Competence and Is Induced Both by Oxidative Stress and by Approach to Stationary Phase

Journal of Bacteriology ◽

10.1128/jb.180.8.2087-2092.1998 ◽

1998 ◽

Vol 180 (8) ◽

pp. 2087-2092 ◽

Cited By ~ 95

Author(s):

Karen L. Visick ◽

Edward G. Ruby

Keyword(s):

Hydrogen Peroxide ◽

Stationary Phase ◽

Catalase Activity ◽

Consensus Sequence ◽

Start Codon ◽

Predicted Amino Acid Sequence ◽

Wild Type ◽

Group Iii ◽

E Coli ◽

Catalase Gene

ABSTRACT The catalase gene, katA, of the sepiolid squid symbiontVibrio fischeri has been cloned and sequenced. The predicted amino acid sequence of KatA has a high degree of similarity to the recently defined group III catalases, including those found in Haemophilus influenzae, Bacteroides fragilis, and Proteus mirabilis. Upstream of the predicted start codon of katA is a sequence that closely matches the consensus sequence for promoters regulated inEscherichia coli by the alternative sigma factor encoded byrpoS. Further, the level of expression of the clonedkatA gene in an E. coli rpoS mutant is much lower than in wild-type E. coli. Catalase activity is induced three- to fourfold both as growing V. fischericells approach stationary phase and upon the addition of a small amount of hydrogen peroxide during logarithmic growth. The catalase activity was localized in the periplasm of wild-type V. fischeri cells, where its role could be to detoxify hydrogen peroxide coming from the external environment. No significant catalase activity could be detected in a katA null mutant strain, demonstrating that KatA is the predominately expressed catalase inV. fischeri and indicating that V. fischeri carries only a single catalase gene. The catalase mutant was defective in its ability to competitively colonize the light organs of juvenile squids in coinoculation experiments with the parent strain, suggesting that the catalase enzyme plays an important role in the symbiosis between V. fischeri and its squid host.

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Decomposition of hydrogen peroxide on cerium dioxide-nickel oxide two-component catalysts and the effect of ionizing radiation on them

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19840014 ◽

1984 ◽

Vol 49 (1) ◽

pp. 14-24 ◽

Cited By ~ 6

Author(s):

Viliam Múčka

Keyword(s):

Heat Treatment ◽

Hydrogen Peroxide ◽

Ionizing Radiation ◽

Nickel Oxide ◽

Cerium Dioxide ◽

Catalytic Properties ◽

Specific Activity ◽

Ion Pairs ◽

Composition Region ◽

Two Component

Some physical and catalytic properties of cerium dioxide-nickel oxide two-component catalysts have been studied over the entire composition region, employing the decomposition of hydrogen peroxide in aqueous solution as a model catalytic process. The two oxides have been found to affect each other, particularly for NiO contents of 9.1 and 96.7 mol%; the mutual influencing, the nature of which in the conditions applied remains unaffected by heat treatment of the sample or by its exposition to ionizing radiation, is manifested by the nonmonotonic dependences of the oxidation power and of the specific activity of the catalysts on their composition. This can be interpreted in terms of the concept of bivalent catalytic centres, assuming that for nickel oxide the centres consist of Ni2+-Ni3+ ion pairs, for cerium dioxide they consist of Ce3+-Ce4+ ion pairs, and that in the region of the mutual influencing , Ni2+-Ce4+ ion pairs play a major role. Within the scope of this concept, the increase in the oxidation power of all the catalysts in question and a simultaneously decrease in the specific activity of the pure nickeloxide exposed to ionizing radiation can be explained in terms of the ionization effect.

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Hydrogen peroxide-responsive AIE probe for imaging-guided organelle targeting and photodynamic cancer cell ablation

Materials Chemistry Frontiers ◽

10.1039/d1qm00328c ◽

2021 ◽

Author(s):

Qian Wu ◽

Youmei Li ◽

Ying Li ◽

Dong Wang ◽

Ben Zhong Tang

Keyword(s):

Reactive Oxygen Species ◽

Hydrogen Peroxide ◽

Cancer Cell ◽

Reactive Oxygen ◽

Living Cells ◽

Oxygen Species ◽

Cell Ablation ◽

Selective Monitoring ◽

Organelle Targeting

Hydrogen peroxide (H2O2), as one kind of key reactive oxygen species (ROS), is mainly produced endogenously primarily in the mitochondria. The selective monitoring of H2O2 in living cells is of...

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Upconversion-based nanosystems for fluorescence sensing of pH and H2O2

Nanoscale Advances ◽

10.1039/d0na01045f ◽

2021 ◽

Author(s):

Chunning Sun ◽

Michael Gradzielski

Keyword(s):

Reactive Oxygen Species ◽

Hydrogen Peroxide ◽

Excitation Energy ◽

Reactive Oxygen ◽

Oxygen Species ◽

Fluorescence Sensing ◽

Living Organisms

Hydrogen peroxide (H2O2), a key reactive oxygen species, plays an important role in living organisms, industrial and environmental fields. Here, a non-contact upconversion nanosystem based on the excitation energy attenuation...

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