Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes

Passardi, Filippo; Bakalovic, Nenad; Teixeira, Felipe Karam; Margis‐Pinheiro, Márcia; Penel, Claude; Dunand, Christophe

doi:10.1016/j.ygeno.2007.01.006

Cited by 104 publications

(96 citation statements)

References 50 publications

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“…The intracellular class I can be found in most living organisms, except animals. Its widespread distribution-in particular its presence in prokaryotes-suggests that class I peroxidases are probably at the origin of the two other classes (Passardi et al, 2007). Their main function in the cell is detoxification of excess H 2 O 2 (Skulachev, 1998;Erman and Vitello, 2002;Shigeoka et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Specific functions of individual class III peroxidase genes

Cosio

Dunand

2009

Journal of Experimental Botany

364

288

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In higher plants, class III peroxidases exist as large multigene families (e.g. 73 genes in Arabidopsis thaliana). The diversity of processes catalysed by peroxidases as well as the large number of their genes suggests the possibility of a functional specialization of each isoform. In addition, the fact that peroxidase promoter sequences are very divergent and that protein sequences contain both highly conserved domains and variable regions supports this hypothesis. However, two difficulties are associated with the study of the function of specific peroxidase genes: (i) the modification of the expression of a single peroxidase gene often results in no visible mutant phenotype, because it is compensated by redundant genes; and (ii) peroxidases show low substrate specificity in vitro resulting in an unreliable indication of peroxidase specific activity unless complementary data are available. The generalization of molecular biology approaches such as whole transcriptome analysis and recombinant DNA combined with biochemical approaches provide unprecedented tools for overcoming these difficulties. This review highlights progress made with these new techniques for identifying the specific function of individual class III peroxidase genes taking as an example the model plant A. thaliana, as well as discussing some other plants.

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Section: Introductionmentioning

confidence: 99%

Specific functions of individual class III peroxidase genes

Cosio

Dunand

2009

Journal of Experimental Botany

364

288

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“…This process contributes to the low nutrient availability in boreal forests, which limits productivity of the ecosystem (Northup et al, 1995). Enzymatic degradation of polyphenolic complexes is mainly carried out by oxidative enzymes, such as laccases and peroxidases (Bao et al, 1993;Passardi et al, 2007a). Both enzymes have a central role in wood decomposition (Rayner et al, 1987), but peroxidases have higher redox potentials than laccases (Baldrian, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…The chelate reacts with polyphenolic substrates, which are oxidized and degraded. A third group of fungal peroxidases has been termed versatile peroxidases (VP; EC 1.11.1.16) and combines the catalytic properties of both LiPs and MnPs (Hatakka, 1994;Martinez, 2002;Passardi et al, 2007a).…”

Section: Introductionmentioning

confidence: 99%

ClassII peroxidase-encoding genes are present in a phylogenetically wide range of ectomycorrhizal fungi

Bödeker

Nygren

Taylor³

et al. 2009

The ISME Journal

158

123

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Fungal peroxidases (ClassII) have a key role in degrading recalcitrant polyphenolic compounds in boreal forest wood, litter and humus. To date, their occurrence and activity have mainly been studied in a small number of white-rot wood decomposers. However, peroxidase activity is commonly measured in boreal forest humus and mineral soils, in which ectomycorrhizal fungi predominate. Here, we used degenerate PCR primers to investigate whether peroxidase-encoding genes are present in the genomes of a wide phylogenetic range of ectomycorrhizal taxa. Cloning and sequencing of PCR products showed that ectomycorrhizal fungi from several different genera possess peroxidase genes. The new sequences represent four major homobasidiomycete lineages, but the majority is derived from Cortinarius, Russula and Lactarius. These genera are ecologically important, but consist mainly of non-culturable species from which little ecophysiological information is available. The amplified sequences contain conserved active sites, both for folding and substrate oxidation. In some Cortinarius spp., there is evidence for gene duplications during the evolution of the genus. ClassII peroxidases seem to be an ancient and a common feature of most homobasidiomycetes, including ectomycorrhizal fungi. Production of extracellular peroxidases may provide ectomycorrhizal fungi with access to nitrogen sequestered in complex polyphenolic sources.

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“…Class I peroxidases exhibited major role in oxidative stress i.e. detoxification of ROS [6]. They include cytochrome c peroxidase, ascorbate peroxidase and catalase peroxidase.…”

Section: Introductionmentioning

confidence: 99%

A Defense Associated Peroxidase from Lemon Having Dye Decolorizing Ability and Offering Resistance to Heat, Heavy Metals and Organic Solvents

Veda¹,

ey²,

Bhagat³

et al. 2016

Biochem Anal Biochem

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Peroxidases have ability to catalyze redox reaction of a wide range of phenolic as well as non-phenolic compounds and exhibited various physiological roles in plant life cycle. From the point of view of industrial applications of peroxidases, the isolation and characterization of peroxidases offering resistance to higher pH and temperature, salts, organic solvents is highly desirable. In this direction, a partial cDNA clone of peroxidase from lemon was isolated and characterized. The peroxidase was found to be defense associated as evident by the higher expression in diseased condition than that of healthy one at both the transcript and enzymatic activity levels. This defense related peroxidase from lemon leaves was purified to homogeneity using quick two step processes of heat treatment and affinity chromatography. The native peroxidase was found to be a heterotrimer of 200 kDa, consisting of two subunits each of 66 kDa while, one subunit of 70 kDa. The purified peroxidase was found to be stable towards heat (retained 92% activity at 80°C for 1 h) and organic solvents, namely ethanol, methanol and isopropanol (retained 30-50% activity in the presence of 50% (v/v) of these solvents for 1 h). Purified peroxidase also exhibited tolerance to heavy metal ions such as Cd 2+ , Ni 2+ and Cs 2+ . The purified lemon peroxidase was found to efficiently oxidize the industrial dyes in the order of aniline blue>methyl orange> indigo carmine >trypan blue > crystal violet, such that 40-54% dye decolorization was observed within 4 h. Thus, the properties exhibited by purified lemon peroxidase make it a promising candidate enzyme for industrial exploitation.

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Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes

Cited by 104 publications

References 50 publications

Specific functions of individual class III peroxidase genes

Specific functions of individual class III peroxidase genes

ClassII peroxidase-encoding genes are present in a phylogenetically wide range of ectomycorrhizal fungi

A Defense Associated Peroxidase from Lemon Having Dye Decolorizing Ability and Offering Resistance to Heat, Heavy Metals and Organic Solvents

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