A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

Ferreira, Patricia; Carro, Juan; Serrano, Ana; Martínez, Ángel T.

doi:10.3852/15-027

Cited by 57 publications

(69 citation statements)

References 119 publications

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“…Mutation of R. leguminosarum gmcA did not affect the growth of free-living bacteria but led to decreased antioxidative capacity under the conditions of 5 and 10 mM hydrogen peroxide H 2 O 2 . The direct link between GmcA and H 2 O 2 detoxification has been less reported, while in most wood-rotting fungi, the members of GMC oxidoreductase superfamily play a central role in the degradation process because they generate extracellular H 2 O 2 , acting as the ultimate oxidizer (Ferreira et al, 2015). Our results suggested that cells with GmcA tolerate internally generated or exogenously applied H 2 O 2 .…”

Section: Discussionmentioning

confidence: 64%

A GMC Oxidoreductase GmcA Is Required for Symbiotic Nitrogen Fixation in Rhizobium leguminosarum bv. viciae

Zou

Luo

et al. 2020

Front. Microbiol.

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GmcA is a FAD-containing enzyme belonging to the GMC (glucose-methanol-choline oxidase) family of oxidoreductases. A mutation in the Rhizobium leguminosarum gmcA gene was generated by homologous recombination. The mutation in gmcA did not affect the growth of R. leguminosarum, but it displayed decreased antioxidative capacity at H 2 O 2 conditions higher than 5 mM. The gmcA mutant strain displayed no difference of glutathione reductase activity, but significantly lower level of the glutathione peroxidase activity than the wild type. Although the gmcA mutant was able to induce the formation of nodules, the symbiotic ability was severely impaired, which led to an abnormal nodulation phenotype coupled to a 30% reduction in the nitrogen fixation capacity. The observation on ultrastructure of 4-week pea nodules showed that the mutant bacteroids tended to start senescence earlier and accumulate poly-β-hydroxybutyrate (PHB) granules. In addition, the gmcA mutant was severely impaired in rhizosphere colonization. Real-time quantitative PCR showed that the gmcA gene expression was significantly up-regulated in all the detected stages of nodule development, and statistically significant decreases in the expression of the redoxin genes katG, katE, and ohrB were found in gmcA mutant bacteroids. LC-MS/MS analysis quantitative proteomics techniques were employed to compare differential gmcA mutant root bacteroids in response to the wild type infection. Sixty differentially expressed proteins were identified including 33 up-regulated and 27 down-regulated proteins. By sorting the identified proteins according to metabolic function, 15 proteins were transporter protein, 12 proteins were related to stress response and virulence, and 9 proteins were related to transcription factor activity. Moreover, nine proteins related to amino acid metabolism were over-expressed.

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Section: Discussionmentioning

confidence: 64%

A GMC Oxidoreductase GmcA Is Required for Symbiotic Nitrogen Fixation in Rhizobium leguminosarum bv. viciae

Zou

Luo

et al. 2020

Front. Microbiol.

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“…For this purpose, fungi secrete H 2 O 2 -generating enzymes, such as glucose oxidases, alcohol oxidases, and aryl-alcohol oxidases (AAOs, EC 1.1.3.7), providing the required H 2 O 2 . They are FAD flavoproteins and belong to the GMC oxidoreductase family within which they are the most abundant members amongst white-rot fungi (Hernández-Ortega et al 2012;Ferreira et al 2015). AAOs produce H 2 O 2 by oxidizing a wide variety of primary aromatic alcohols to aldehydes, such as m-and p-anisyl alcohol, veratryl alcohol, benzyl alcohol, and 5-hydroxymethylfurfural (Guillen et al 1992;Ferreira et al 2005;Feldman et al 2015).…”

Section: Introductionmentioning

confidence: 99%

An aryl-alcohol oxidase of Pleurotus sapidus: heterologous expression, characterization, and application in a 2-enzyme system

Ilya

Javeed

Hanno

et al. 2016

Appl Microbiol Biotechnol

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Aryl-alcohol oxidases (AAOs) are enzymes supporting the degradation of lignin by fungal derived class II peroxidases produced by white-rot fungi. AAOs are able to generate H2O2 as a by-product via oxidation of an aryl-alcohol into its correspondent aldehyde. In this study, an AAO was heterologously expressed in a basidiomycete host for the first time. The gene for an AAO of the white-rot fungus Pleurotus sapidus, a close relative to the oyster mushroom Pleurotus ostreatus, was cloned into an expression vector and put under control of the promotor of the glyceraldehyde-3-phosphate dehydrogenase gene 2 (gpdII) of the button mushroom Agaricus bisporus. The expression vector was transformed into the model basidiomycete Coprinopsis cinerea, and several positive transformants were obtained. The best producing transformants were grown in shake-flasks and in a stirred tank reactor reaching enzymatic activities of up to 125 U L(-1) using veratryl alcohol as a substrate. The purified AAO was biochemically characterized and compared to the previously described native and recombinant AAOs from other Pleurotus species. In addition, a two-enzyme system comprising a dye-decolorizing peroxidase (DyP) from Mycetinis scorodonius and the P. sapidus AAO was successfully employed to bleach the anthraquinone dye Reactive Blue 5.

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“…These oxidoreductases are enzymes of CAZy auxiliary activity family 2 (AA2) [8] fungal class-II lignin-modifying peroxidases including lignin peroxidases (LiPs), manganese peroxidases (MnPs), and versatile peroxidases (VPs) that are important in lignin modification [2, 9, 10]. Class-II peroxidases require hydrogen peroxide which may be generated by other CAZy auxiliary activity enzymes belonging to copper radical oxidases (CROs, AA5) and glucose–methanol–choline superfamily (GMCs, AA3) oxidoreductases [11, 12]. Lignin-converting enzyme set also includes the dye-decolorizing peroxidases (DyPs) [10, 13] and laccases.…”

Section: Introductionmentioning

confidence: 99%

Time-scale dynamics of proteome and transcriptome of the white-rot fungus Phlebia radiata: growth on spruce wood and decay effect on lignocellulose

Kuuskeri

Häkkinen

Laine

et al. 2016

Biotechnol Biofuels

103

139

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BackgroundThe white-rot Agaricomycetes species Phlebia radiata is an efficient wood-decaying fungus degrading all wood components, including cellulose, hemicellulose, and lignin. We cultivated P. radiata in solid state cultures on spruce wood, and extended the experiment to 6 weeks to gain more knowledge on the time-scale dynamics of protein expression upon growth and wood decay. Total proteome and transcriptome of P. radiata were analyzed by peptide LC–MS/MS and RNA sequencing at specific time points to study the enzymatic machinery on the fungus’ natural growth substrate.ResultsAccording to proteomics analyses, several CAZy oxidoreductase class-II peroxidases with glyoxal and alcohol oxidases were the most abundant proteins produced on wood together with enzymes important for cellulose utilization, such as GH7 and GH6 cellobiohydrolases. Transcriptome additionally displayed expression of multiple AA9 lytic polysaccharide monooxygenases indicative of oxidative cleavage of wood carbohydrate polymers. Large differences were observed for individual protein quantities at specific time points, with a tendency of enhanced production of specific peroxidases on the first 2 weeks of growth on wood. Among the 10 class-II peroxidases, new MnP1-long, characterized MnP2-long and LiP3 were produced in high protein abundances, while LiP2 and LiP1 were upregulated at highest level as transcripts on wood together with the oxidases and one acetyl xylan esterase, implying their necessity as primary enzymes to function against coniferous wood lignin to gain carbohydrate accessibility and fungal growth. Majority of the CAZy encoding transcripts upregulated on spruce wood represented activities against plant cell wall and were identified in the proteome, comprising main activities of white-rot decay.ConclusionsOur data indicate significant changes in carbohydrate-active enzyme expression during the six-week surveillance of P. radiata growing on wood. Response to wood substrate is seen already during the first weeks. The immediate oxidative enzyme action on lignin and wood cell walls is supported by detected lignin substructure sidechain cleavages, release of phenolic units, and visual changes in xylem cell wall ultrastructure. This study contributes to increasing knowledge on fungal genetics and lignocellulose bioconversion pathways, allowing us to head for systems biology, development of biofuel production, and industrial applications on plant biomass utilizing wood-decay fungi.Electronic supplementary materialThe online version of this article (doi:10.1186/s13068-016-0608-9) contains supplementary material, which is available to authorized users.

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A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes

Cited by 57 publications

References 119 publications

A GMC Oxidoreductase GmcA Is Required for Symbiotic Nitrogen Fixation in Rhizobium leguminosarum bv. viciae

A GMC Oxidoreductase GmcA Is Required for Symbiotic Nitrogen Fixation in Rhizobium leguminosarum bv. viciae

An aryl-alcohol oxidase of Pleurotus sapidus: heterologous expression, characterization, and application in a 2-enzyme system

Time-scale dynamics of proteome and transcriptome of the white-rot fungus Phlebia radiata: growth on spruce wood and decay effect on lignocellulose

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