The in Vivo and in Vitro Inhibition of Catalase from Leaves of Nicotiana sylvestris by 3-Amino-1,2,4-Triazole

Havir, Evelyn A.

doi:10.1104/pp.99.2.533

Cited by 42 publications

(23 citation statements)

References 25 publications

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“…54). The amitrole concentration used (20 mM) was optimum for inhibiting different plant catalase isozymes (70) and resulted in a massive increase in expression of different carotenogenic gene transcripts (Fig. 3C).…”

Section: Down-regulation Of Ros-scavenging Enzymes Induces the Expresmentioning

confidence: 99%

Induction and Control of Chromoplast-specific Carotenoid Genes by Oxidative Stress

Bouvier¹,

Backhaus²,

Camara³

1998

Journal of Biological Chemistry

186

102

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The differentiation of chloroplasts into chromoplasts involves a series of biochemical changes that culminate with the intense accumulation of long chain chromophore carotenoids such as lycopene, rhodoxanthin, astaxanthin, anhydroeschsoltzxanthin, capsanthin, and capsorubin. The signal pathways mediating these transformations are unknown. Chromoplast carotenoids are known to accumulate in green tissues experiencing stress conditions, and studies indicate that they provide efficient protection against oxidative stress. We tested the role of reactive oxygen species (ROS) as regulators of chromoplast carotenoid biosynthesis in vivo. The addition of ROS progenitors, such as menadione, tert-butylhydroperoxide, or paraquat and prooxidants such as diamide or buthionine sulfoximine to green pericarp discs of pepper fruits rapidly and dramatically induce the simultaneous expression of multiple carotenogenic gene mRNAS that give rise to capsanthin. Similarly, down-regulation of catalase by amitrole induces expression of carotenogenic gene mRNAs leading to the synthesis of capsanthin in excised green pericarp discs. ROS signals from plastids and mitochondria also contribute significantly to this process. Analysis of the capsanthin-capsorubin synthase promoter in combination with a ␤-glucuronidase reporter gene reveals strong activation in transformed pepper protoplasts challenged with the above ROS. Collectively these data demonstrate that ROS act as a novel class of second messengers that mediate intense carotenoid synthesis during chromoplast differentiation.Plastids are plant organelles whose diverse functions include photosynthesis, gravity perception, and biogenesis of microand macromolecules. These functions do not occur in all plastids but are associated with structurally distinct plastid types. Plastid differentiation is a highly coordinated process involving programmed, multi-phase events that are transduced by a variety of stimuli. These transducers activate numerous morphological and biochemical changes that ultimately affect plastid compartmentalization. This is particularly evident in chloroplasts undergoing the transformation to chromoplasts, an event characterized by the synthesis and accumulation of carotenoids into unique plastid substructures. These changes are accompanied by the yellow to red color shift in flowers, fruits, and roots of certain plants (1, 2). Although the molecular events controlling these alterations are largely unknown, emerging evidence suggests that reactive oxygen species (ROS) 1 may play a vital role in this process (3). In this paper we present data showing how oxidative stress affects carotenogenesis in plants.Data from several model systems indicate that ROS operate at the molecular level. Homeostatic variations in ROS levels are known to activate normal and pathological events during animal cell development (4, 5).

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Section: Down-regulation Of Ros-scavenging Enzymes Induces the Expresmentioning

confidence: 99%

Induction and Control of Chromoplast-specific Carotenoid Genes by Oxidative Stress

Bouvier¹,

Backhaus²,

Camara³

1998

Journal of Biological Chemistry

186

102

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“…This assay condition with a low level of H 2 O 2 closely mimics the in vivo situation, in which H 2 O 2 is continuously being produced by various metabolic pathways, including photorespiration in leaves. Inclusion of a low level of H 2 O 2 in the preincubation mixture has also been used for assaying catalase inhibition by other phenolic compounds (Ogura et al, 1950) and 3-aminotriazole (Havir, 1992). Thus, soluble proteins were first preincubated for 1 h in a 100-/xL mixture consisting of 20 mM citrate, pH 6.5, 0.05% Glc, 5 milliunits of Glc oxidase, 1 mM SA, and 5 to 50 jig of protein, depending on the tissues.…”

Section: Catalase Assaysmentioning

confidence: 99%

“…, 1992Enyedi et al, 1992), Arabidopsis Bowling et al, 1994;Dietrich et al, 1994;Greenberg et al, 1994;Weyman et al, 1995), and cucumber (Metraux et al, 1990;Rasmussen et al, 1991). Further evidence for the involvement of SA in the induction of defense responses is provided by transgenic tobacco and Arabidopsis plants that constitutively express the nahG gene encoding a salicylate hydroxylase from Pseudomonas putida (Gaffney et al, 1993;Delaney et al, 1994).…”

mentioning

confidence: 99%

Differential Accumulation of Salicylic Acid and Salicylic Acid-Sensitive Catalase in Different Rice Tissues

et al. 1997

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We previously proposed that salicylic acid (SA)-sensitive catalases serve as biological targets of SA in plant defense responses. To further examine the role of SA-sensitive catalases, we have analyzed the relationship between SA levels and SA sensitivity of catalases in different rice (Oryza saliva) tissues. We show here that, whereas rice shoots contain extremely high levels of free SA, as previously reported ( , rice roots and cell-suspension cultures have very low SA levels. Catalases from different rice tissues also exhibit differences in sensitivity to SA. Catalase from rice shoots is insensitive to SA, but roots and cell-suspension cultures contain SA-sensitive catalase. The difference in SA sensitivity of catalases from these different tissues correlates with the tissue-specific expression of two catalase genes, CafA and CafB, which encode highly distinctive catalase proteins. CafA, which encodes a catalase with relatively low sequence homology to the tobacco SA-sensitive catalases, is expressed at high levels exclusively in the shoots. On the other hand, in roots and cell-suspension cultures, with northern analysis we detected expression of only the CafB gene, which encodes a catalase with higher sequence homology to tobacco catalases. The role of catalases in mediating some of the SA-induced responses is discussed in light of these results and the recently defined mechanisms of catalase inhibition by SA.

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“…In addition, catalase activity was completely lost when the recombinant proteins were incubated in the presence of 1 mM potassium cyanide, whereas 3-amino-1,2,4-triazole (3-AT) at 0.1 or 1.0 mM resulted in only marginal reductions in catalase activity in OsCatA and OsCatC and a small reduction in OsCatB. 3-AT is a specific inhibitor of CAT activity, both in vivo and in vitro, [32][33][34] but similar results as to the relatively weak sensitivity to 3-AT have been found for catalase isozymes isolated from Z. mays 11) and tobacco (Nicotiana sylvestris).…”

Section: Effects Of Inhibitors On Catalase Activitymentioning

confidence: 99%

Cloning and Characterization of Catalases from Rice,Oryza sativaL.

Wutipraditkul¹,

Boonkomrat²,

Buaboocha³

2011

Bioscience, Biotechnology, and Biochemistry

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Catalase is the major H 2 O 2 -scavenging enzyme in all aerobic organisms. From the cDNA sequences of three rice (Oryza sativa L.) genes that encode for predicted catalases (OsCatA, OsCatB, and OsCatC), complete ORFs were subcloned into pET21a and expressed as (His) 6 -tagged proteins in Escherichia coli. The recombinant (His) 6 -polypeptides were enriched to apparent homogeneity and characterized. With H 2 O 2 as substrate, the highest catalase k cat value (20 AE 1:71 Â 10 À3 min À1 ) was found in recombinant OsCatB. The optimum temperatures for catalase activity were 30 C for OsCatA and OsCatC and 25 C for OsCatB, while the pH optima were 8.0, 7.5, and 7.0 for OsCatA, OsCatB, and OsCatC respectively. All the catalases were inhibited by sodium azide, -mercaptoethanol, and potassium cyanide, but only weakly by 3-amino-1,2,4-triazole. The various catalases exhibited different catalase activities in the presence of different salts at different concentrations, OsCatC showing higher salt inhibitory effects than the two other OsCats.

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The in Vivo and in Vitro Inhibition of Catalase from Leaves of Nicotiana sylvestris by 3-Amino-1,2,4-Triazole

Cited by 42 publications

References 25 publications

Induction and Control of Chromoplast-specific Carotenoid Genes by Oxidative Stress

Induction and Control of Chromoplast-specific Carotenoid Genes by Oxidative Stress

Differential Accumulation of Salicylic Acid and Salicylic Acid-Sensitive Catalase in Different Rice Tissues

Cloning and Characterization of Catalases from Rice,Oryza sativaL.

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