Serveur d'exploration sur le phanerochaete

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Effects of Homologous Expression of 1,4-Benzoquinone Reductase and Homogentisate 1,2-Dioxygenase Genes on Wood Decay in Hyper-Lignin-Degrading Fungus Phanerochaete sordida YK-624.

Identifieur interne : 000212 ( Main/Exploration ); précédent : 000211; suivant : 000213

Effects of Homologous Expression of 1,4-Benzoquinone Reductase and Homogentisate 1,2-Dioxygenase Genes on Wood Decay in Hyper-Lignin-Degrading Fungus Phanerochaete sordida YK-624.

Auteurs : Toshio Mori [Japon] ; Genki Koyama [Japon] ; Hirokazu Kawagishi [Japon] ; Hirofumi Hirai [Japon]

Source :

RBID : pubmed:27363425

Descripteurs français

English descriptors

Abstract

We investigated the function of 1,4-benzoquinone reductase (BQR)- and homogentisate 1,2-dioxygenase (HGD)-like genes in wood degradation by Phanerochaete sordida YK-624, which exhibits high ligninolytic activity and selectivity. We determined homologous expression in the genomic and cDNA sequences of BQR- and HGD-like genes in P. sordida YK-624 (PsBQR and PsHGD). Both genes shared high homology (≥90 % amino acid sequence similarity) with the corresponding genes in Phanerochaete chrysosporium. These genes were co-transformed with a reporter gene into an uracil auxotrophic mutant of P. sordida YK-624. The PsBQR and PsHGD co-transformants exhibited lower holocellulolytic activity and higher ligninolytic selectivity than the control transformants. In liquid culture with vanillin, both co-transformants significantly accelerated vanillin degradation. Thus, we suggest that the rapid metabolism of low-molecular weight lignin fragments, due to the homologous expression of BQR- and HGD-like genes, affects quinone redox cycling to produce hydroxyl radicals, thereby decreasing holocellulose degradation and increasing ligninolytic selectivity.

DOI: 10.1007/s00284-016-1089-6
PubMed: 27363425


Affiliations:


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Le document en format XML

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<term>Cloning, Molecular (MeSH)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Homogentisate 1,2-Dioxygenase (genetics)</term>
<term>Homogentisate 1,2-Dioxygenase (metabolism)</term>
<term>Lignin (metabolism)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Phanerochaete (metabolism)</term>
<term>Quinone Reductases (genetics)</term>
<term>Quinone Reductases (metabolism)</term>
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<term>Benzaldéhydes (métabolisme)</term>
<term>Bois (microbiologie)</term>
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<term>Homogentisate 1,2-dioxygenase (génétique)</term>
<term>Homogentisate 1,2-dioxygenase (métabolisme)</term>
<term>Lignine (métabolisme)</term>
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<term>Phanerochaete (métabolisme)</term>
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<term>Protéines fongiques (métabolisme)</term>
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<term>Quinone reductases (métabolisme)</term>
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<term>Fungal Proteins</term>
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<term>Quinone Reductases</term>
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<term>Fungal Proteins</term>
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<term>Quinone Reductases</term>
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<term>Phanerochaete</term>
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<term>Quinone reductases</term>
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<div type="abstract" xml:lang="en">We investigated the function of 1,4-benzoquinone reductase (BQR)- and homogentisate 1,2-dioxygenase (HGD)-like genes in wood degradation by Phanerochaete sordida YK-624, which exhibits high ligninolytic activity and selectivity. We determined homologous expression in the genomic and cDNA sequences of BQR- and HGD-like genes in P. sordida YK-624 (PsBQR and PsHGD). Both genes shared high homology (≥90 % amino acid sequence similarity) with the corresponding genes in Phanerochaete chrysosporium. These genes were co-transformed with a reporter gene into an uracil auxotrophic mutant of P. sordida YK-624. The PsBQR and PsHGD co-transformants exhibited lower holocellulolytic activity and higher ligninolytic selectivity than the control transformants. In liquid culture with vanillin, both co-transformants significantly accelerated vanillin degradation. Thus, we suggest that the rapid metabolism of low-molecular weight lignin fragments, due to the homologous expression of BQR- and HGD-like genes, affects quinone redox cycling to produce hydroxyl radicals, thereby decreasing holocellulose degradation and increasing ligninolytic selectivity. </div>
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