In Vitro Assembly of Catalase

Baureder, Michael; Barane, Elisabeth; Hederstedt, Lars

doi:10.1074/jbc.m114.596148

Cited by 24 publications

(17 citation statements)

References 23 publications

(40 reference statements)

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“…One recent in vitro study using Enterococcus faecalis catalase demonstrated the importance of heme insertion in formation of tetrameric active catalase(14). To understand heme maturation of catalase in mammalian cells, we utilized our previous finding of NO-mediated inhibition of heme maturation into catalase to identify factors regulating its heme incorporation and therefore tetramerization to make the active enzyme.…”

Section: Discussionmentioning

confidence: 99%

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Novel insights in mammalian catalase heme maturation: Effect of NO and thioredoxin-1

Chakravarti

Gupta

Majors

et al. 2015

Free Radical Biology and Medicine

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Catalase is a tetrameric heme-containing enzyme with essential antioxidant functions in biology. Multiple factors including nitric oxide (NO) have been shown to attenuate its activity. However, the possible impact of NO in relation to the maturation of active catalase, including its heme acquisition and tetramer formation, has not been investigated. We found that NO attenuates heme insertion into catalase in both short-term and long-term incubations. The NO inhibition in catalase heme incorporation was associated with defective oligomerization of catalase, such that inactive catalase monomers and dimers accumulated in place of the mature tetrameric enzyme. We also found that GAPDH plays a key role in mediating these NO effects on the structure and activity of catalase. Moreover, the NO sensitivity of catalase maturation could be altered up or down by manipulating the cellular expression level or activity of thioredoxin-1, a known protein-SNO denitrosylase enzyme. In a mouse model of allergic inflammatory asthma, we found that lungs from allergen-challenged mice contained a greater percentage of dimeric catalase relative to tetrameric catalase in the unchallenged control, suggesting that the mechanisms described here are in play in the allergic asthma model. Together, our study shows how maturation of active catalase can be influenced by NO, S-nitrosylated GAPDH, and thioredoxin-1, and how maturation may become compromised in inflammatory conditions such as asthma.

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Section: Discussionmentioning

confidence: 99%

“…In rat liver apo-catalase is present in 3 fold excess (1.6% compared to 0.5%) of holo-monomeric catalase (13). Lack of heme can increase the pool of apo-catalase and may promote its turnover (14,15). Exposure to oxidative stress can inactivate catalase (16-19), but whether this affects its structure is not completely understood.…”

Section: Introductionmentioning

confidence: 99%

Novel insights in mammalian catalase heme maturation: Effect of NO and thioredoxin-1

Chakravarti

Gupta

Majors

et al. 2015

Free Radical Biology and Medicine

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“…Being a heme-catalase, KatB (EC 1.11.1.6) depends on its co-factor, heme, for the enzymatic activity of reducing H 2 O 2 to H 2 O [41]. However, the production of monomeric apo-catalase does not rely on heme [42]. Given that iron availability has no impact on catalase expression in V. cholerae [43], we hypothesized that iron content would affect catalase activity at the post-translational level, which could be partially compensated by CBS-derived H 2 S. To test this hypothesis, we examined the impact of cbs expression on KatB activity in V. cholerae cells under iron-deficient (achieved by supplementation of iron chelator 2,2'-bipyridine) or iron-enriched (achieved by supplementation of FeCl 3 ) conditions.…”

Section: Plos Pathogensmentioning

confidence: 99%

CBS-derived H2S facilitates host colonization of Vibrio cholerae by promoting the iron-dependent catalase activity of KatB

Yang

Wang

et al. 2021

PLoS Pathog

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Sensing and resisting oxidative stress is critical for Vibrio cholerae to survive in either the aquatic environment or the gastrointestinal tract. Previous studies mainly focused on the mechanisms of oxidative stress response regulation that rely on enzymatic antioxidant systems, while functions of non-enzymatic antioxidants are rarely discussed in V. cholerae. For the first time, we investigated the role of hydrogen sulfide (H2S), the simplest thiol compound, in protecting V. cholerae against oxidative stress. We found that degradation of L-cysteine by putative cystathionine β-synthase (CBS) is the major source of endogenous H2S in V. cholerae. Our results indicate that intracellular H2S level has a positive correlation with cbs expression, while the enhanced H2S production can render V. cholerae cells less susceptible to H2O2 in vitro. Using proteome analysis and real-time qPCR assay, we found that cbs expression could stimulate the expression of several enzymatic antioxidants, including reactive oxygen species (ROS) detoxifying enzymes SodB, KatG and AhpC, the DNA protective protein DPS and the protein redox regulator Trx1. Assays of ROS detoxification capacities revealed that CBS-derived H2S could promote catalase activity at the post-translational level, especially for KatB, which serves as an important way that endogenous H2S participates in H2O2 detoxification. The enhancement of catalase activity by H2S is achieved through facilitating the uptake of iron. Adult mice experiments showed that cbs mutant has colonization defect, while either complementation of cbs or exogenous supplement of N-Acetyl-L-Cysteine restores its fitness in the host environment. Herein, we proposed that V. cholerae regulates CBS-dependent H2S production for better survival and proliferation under ROS stress.

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“…The rate of hydrogen peroxide decomposition at 37 °C was recorded as the decrease in absorption at 240 nm, and activity was calculated based on the initial rate (up to 20 s). One unit was defined as the decomposition of 1 μmol of hydrogen peroxide per minute …”

Section: Methodsmentioning

confidence: 99%

Virulence markers of opportunistic black yeast in Exophiala

Sav

Özakkaş

Altinbaş

et al. 2016

Mycoses

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The black yeast genus Exophiala is known to cause a wide variety of diseases in severely ill individuals but can also affect immunocompetent individuals. Virulence markers and other physiological parameters were tested in eight clinical and 218 environmental strains, with a specific focus on human-dominated habitats for the latter. Urease and catalase were consistently present in all samples; four strains expressed proteinase and three strains expressed DNase, whereas none of the strains showed phospholipase, haemolysis, or co-haemolysis activities. Biofilm formation was identified in 30 (13.8%) of the environmental isolates, particularly in strains from dishwashers, and was noted in only two (25%) of the clinical strains. These results indicate that virulence factors are inconsistently present in the investigated Exophiala species, suggesting opportunism rather than pathogenicity.

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In Vitro Assembly of Catalase

Cited by 24 publications

References 23 publications

Novel insights in mammalian catalase heme maturation: Effect of NO and thioredoxin-1

Novel insights in mammalian catalase heme maturation: Effect of NO and thioredoxin-1

CBS-derived H2S facilitates host colonization of Vibrio cholerae by promoting the iron-dependent catalase activity of KatB

Virulence markers of opportunistic black yeast in Exophiala

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