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    Author(s): Shingo Miyauchi; Hayat Hage; Elodie Drula; Laurence Lesage-Meessen; Jean-Guy Berrin; David Navarro; Anne Favel; Delphine Chaduli; Sacha Grisel; Mireille Haon; François Piumi; Anthony Levasseur; Anne Lomascolo; Steven Ahrendt; Kerrie Barry; Kurt LaButti; Didier Chevret; Chris Daum; Jérôme Mariette; Christophe Klopp; Daniel Cullen; Ronald de Vries; Allen Gathman; Matthieu Hainaut; Bernard Henrissat; Kristiina Hildén; Ursula Kües; Walt Lilly; Anna Lipzen; Miia Mäkelä; Angel Martinez; Mélanie Morel-Rouhier; Emmanuelle Morin; Jasmyn Pangilinan; Arthur Ram; Han Wösten; Francisco Ruiz-Dueñas; Robert Riley; Eric Record; Igor Grigoriev; Marie-Noëlle Rosso
    Date: 2020
    Source: DNA Research. 27(2). 14 p.
    Publication Series: Scientific Journal (JRNL)
    Station: Forest Products Laboratory
    PDF: Download Publication  (1.0 MB)

    Related Research Highlights

    Gene Conservation Among Lignocellulose-Degrading Fungi


    White-rot (WR) fungi are pivotal decomposers of dead organic matter in forest ecosystems and typically use a large array of hydrolytic and oxidative enzymes to deconstruct lignocellulose. However, the extent of lignin and cellulose degradation may vary between species and wood type. Here, we combined comparative genomics, transcriptomics and secretome proteomics to identify conserved enzymatic signatures at the onset of wood-decaying activity within the Basidiomycota genus Pycnoporus. We observed a strong conservation in the genome structures and the repertoires of protein-coding genes across the four Pycnoporus species described to date, despite the species having distinct geographic distributions. We further analysed the early response of P. cinnabarinus, P. coccineus and P. sanguineus to diverse (ligno)-cellulosic substrates. We identified a conserved set of enzymes mobilized by the three species for breaking down cellulose, hemicellulose and pectin. The co-occurrence in the exo-proteomes of H2O2-producing enzymes with H2O2-consuming enzymes was a common feature of the three species, although each enzymatic partner displayed independent transcriptional regulation. Finally, cellobiose dehydrogenase-coding genes were systematically co-regulated with at least one AA9 lytic polysaccharide monooxygenase gene, indicative of enzymatic synergy in vivo. This study highlights a conserved core white-rot fungal enzymatic mechanism behind the wood-decaying process.

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    • This article was written and prepared by U.S. Government employees on official time, and is therefore in the public domain.


    Miyauchi, Shingo; Hage, Hayat; Drula, Elodie; Lesage-Meessen, Laurence; Berrin, Jean-Guy; Navarro, David; Favel, Anne; Chaduli, Delphine; Grisel, Sacha; Haon, Mireille; Piumi, François; Levasseur, Anthony; Lomascolo, Anne; Ahrendt, Steven; Barry, Kerrie; LaButti, Kurt M; Chevret, Didier; Daum, Chris; Mariette, Jérôme; Klopp, Christophe; Cullen, Daniel; de Vries, Ronald P; Gathman, Allen C; Hainaut, Matthieu; Henrissat, Bernard; Hildén, Kristiina S; Kües, Ursula; Lilly, Walt; Lipzen, Anna; Mäkelä, Miia R; Martinez, Angel T; Morel-Rouhier, Mélanie; Morin, Emmanuelle; Pangilinan, Jasmyn; Ram, Arthur F J; Wösten, Han A B; Ruiz-Dueñas, Francisco J; Riley, Robert; Record, Eric; Grigoriev, Igor V; Rosso, Marie-Noëlle. 2020. Conserved white-rot enzymatic mechanism for wood decay in the Basidiomycota genus Pycnoporus. DNA Research. 27(2). 14 p.


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    Wood decay, lignocellulose, CAZyme, lytic polysaccharide monooxygenase, Class II Peroxidase

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