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Widespread occurrence of expressed fungal secretory peroxidases in forest soils.

Identifieur interne : 000015 ( PubMed/Curation ); précédent : 000014; suivant : 000016

Widespread occurrence of expressed fungal secretory peroxidases in forest soils.

Auteurs : Harald Kellner [Allemagne] ; Patricia Luis [France] ; Marek J. Pecyna [Allemagne] ; Florian Barbi [France] ; Danuta Kapturska [Allemagne] ; Dirk Krüger [Allemagne] ; Donald R. Zak [États-Unis] ; Roland Marmeisse [France] ; Micheline Vandenbol [Belgique] ; Martin Hofrichter [Allemagne]

Source :

RBID : pubmed:24763280

English descriptors

Abstract

Fungal secretory peroxidases mediate fundamental ecological functions in the conversion and degradation of plant biomass. Many of these enzymes have strong oxidizing activities towards aromatic compounds and are involved in the degradation of plant cell wall (lignin) and humus. They comprise three major groups: class II peroxidases (including lignin peroxidase, manganese peroxidase, versatile peroxidase and generic peroxidase), dye-decolorizing peroxidases, and heme-thiolate peroxidases (e.g. unspecific/aromatic peroxygenase, chloroperoxidase). Here, we have repeatedly observed a widespread expression of all major peroxidase groups in leaf and needle litter across a range of forest ecosystems (e.g. Fagus, Picea, Acer, Quercus, and Populus spp.), which are widespread in Europe and North America. Manganese peroxidases and unspecific peroxygenases were found expressed in all nine investigated forest sites, and dye-decolorizing peroxidases were observed in five of the nine sites, thereby indicating biological significance of these enzymes for fungal physiology and ecosystem processes. Transcripts of selected secretory peroxidase genes were also analyzed in pure cultures of several litter-decomposing species and other fungi. Using this information, we were able to match, in environmental litter samples, two manganese peroxidase sequences to Mycena galopus and Mycena epipterygia and one unspecific peroxygenase transcript to Mycena galopus, suggesting an important role of this litter- and coarse woody debris-dwelling genus in the disintegration and transformation of litter aromatics and organic matter formation.

DOI: 10.1371/journal.pone.0095557
PubMed: 24763280

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Le document en format XML

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<div type="abstract" xml:lang="en">Fungal secretory peroxidases mediate fundamental ecological functions in the conversion and degradation of plant biomass. Many of these enzymes have strong oxidizing activities towards aromatic compounds and are involved in the degradation of plant cell wall (lignin) and humus. They comprise three major groups: class II peroxidases (including lignin peroxidase, manganese peroxidase, versatile peroxidase and generic peroxidase), dye-decolorizing peroxidases, and heme-thiolate peroxidases (e.g. unspecific/aromatic peroxygenase, chloroperoxidase). Here, we have repeatedly observed a widespread expression of all major peroxidase groups in leaf and needle litter across a range of forest ecosystems (e.g. Fagus, Picea, Acer, Quercus, and Populus spp.), which are widespread in Europe and North America. Manganese peroxidases and unspecific peroxygenases were found expressed in all nine investigated forest sites, and dye-decolorizing peroxidases were observed in five of the nine sites, thereby indicating biological significance of these enzymes for fungal physiology and ecosystem processes. Transcripts of selected secretory peroxidase genes were also analyzed in pure cultures of several litter-decomposing species and other fungi. Using this information, we were able to match, in environmental litter samples, two manganese peroxidase sequences to Mycena galopus and Mycena epipterygia and one unspecific peroxygenase transcript to Mycena galopus, suggesting an important role of this litter- and coarse woody debris-dwelling genus in the disintegration and transformation of litter aromatics and organic matter formation.</div>
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<RefSource>Appl Microbiol Biotechnol. 2000 Apr;53(4):441-6</RefSource>
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<RefSource>Proc Natl Acad Sci U S A. 2012 Oct 23;109(43):17501-6</RefSource>
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<RefSource>Appl Environ Microbiol. 2002 Jul;68(7):3442-8</RefSource>
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