An endo-1,4-β-xylanase-encoding gene from Agaricus bisporus is regulated by compost-specific factors

Groot, Piet W. J. de; Basten, Daniëlle E. J. W.; Sonnenberg, A.S.M.; Griensven, L. J. L. D. van; Visser, Jaap; Schaap, Peter J.

doi:10.1006/jmbi.1997.1605

Cited by 34 publications

(16 citation statements)

References 31 publications

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“…Alternatively, it is possible that abf 62A is expressed by P. cellulosa, but only in complex environments, and is not simply induced by the presence of the substrate. This is consistent with a recent study [24] which showed that an Aspergillus GH10 xylanase was not induced by its target substrate in monoculture, but was expressed when the fungus was inoculated into compost, a highly complex environment both in terms of the nutrients present and the structure of its microbial community. Nevertheless, the possibility that abf 62A is not expressed in P. cellulosa requires that we re-evaluate the general assumption that cloned genes encoding functional plant-cell-wall hydrolases, esterases and lyases are functional in their target host.…”

Section: Discussionsupporting

confidence: 93%

Pseudomonas cellulosa expresses a single membrane-bound glycoside hydrolase family 51 arabinofuranosidase

BEYLOT

Emami

McKie

et al. 2001

Biochemical Journal

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In the accompanying paper [Beylot, McKie, Voragen, DoeswijkVoragen and Gilbert (2001) Biochem. J. 358, 607-614] the chromosome of Pseudomonas cellulosa was shown to contain two genes, abf 51A and abf62A, that encode arabinofuranosidases belonging to glycoside hydrolase families 51 and 62, respectively. In this report we show that expression of Abf 51A is induced by arabinose and arabinose-containing polysaccharides. Northernblot analysis showed that abf 51A was efficiently transcribed, whereas no transcript derived from abf62A was detected in the presence of arabinose-containing polysaccharides. Zymogram and Western-blot analyses revealed that Abf 51A was located on the outer membrane of P. cellulosa. To investigate the importance of Abf 51A in the release of arabinose from poly-and oligosaccharides, transposon mutagenesis was used to construct an

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Section: Discussionsupporting

confidence: 93%

Pseudomonas cellulosa expresses a single membrane-bound glycoside hydrolase family 51 arabinofuranosidase

BEYLOT

Emami

McKie

et al. 2001

Biochemical Journal

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“…For example, certain cellulolytic genes are inhibited by lactose, xylose, mannose, and fructose (89,186,189). Like ascomycetes, the xynA endoxylanase gene of A. bisporus is repressed by glucose (190).…”

Section: Repression Of Gene Expression In Basidiomycetesmentioning

confidence: 99%

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

355

287

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SUMMARY Basidiomycete fungi subsist on various types of plant material in diverse environments, from living and dead trees and forest litter to crops and grasses and to decaying plant matter in soils. Due to the variation in their natural carbon sources, basidiomycetes have highly varied plant-polysaccharide-degrading capabilities. This topic is not as well studied for basidiomycetes as for ascomycete fungi, which are the main sources of knowledge on fungal plant polysaccharide degradation. Research on plant-biomass-decaying fungi has focused on isolating enzymes for current and future applications, such as for the production of fuels, the food industry, and waste treatment. More recently, genomic studies of basidiomycete fungi have provided a profound view of the plant-biomass-degrading potential of wood-rotting, litter-decomposing, plant-pathogenic, and ectomycorrhizal (ECM) basidiomycetes. This review summarizes the current knowledge on plant polysaccharide depolymerization by basidiomycete species from diverse habitats. In addition, these data are compared to those for the most broadly studied ascomycete genus, Aspergillus , to provide insight into specific features of basidiomycetes with respect to plant polysaccharide degradation.

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“…2). During fruit body development, CEL4 follows a profile similar to that of cellulase activity (38) and endoxylanase activity (7,34).…”

Section: Vol 67 2001mentioning

confidence: 97%

“…cel4 has 12 introns ranging from 46 to 65 bp. The other hemicellulase gene sequenced from A. bisporus, xylanase (accession number X78330 [7]), also has a large number of introns (11), while the cellulase genes do not (4,24). The Congo Red plate assays and reducing sugar assays showed that CEL4 protein is a specific mannanase that, when expressed in S. cerevisiae, has no detectable activity against CMC, xylan, or barley ␤-glucan.…”

Section: Vol 67 2001mentioning

confidence: 99%

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The cel4 Gene of Agaricus bisporus Encodes a β-Mannanase

Tang

Waterman

Smith

et al. 2001

Appl Environ Microbiol

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Mannases have industrial uses in food and pulp industries, and their regulation may influence development of the mushrooms of commercially important basidiomycetes. We expressed an Agaricus bisporus cel4 cDNA, which encodes a mannanase, in Saccharomyces cerevisiae and Pichia pastoris. CEL4 had no detectable activity on cellulose or xylan. This gene is the first isolated from this economically important fungus to encode a mannanase. P. pastoris secreted about three times more CEL4 than S. cerevisiae. The removal of the cellulosebinding domain of CEL4 lowered the secreted specific activity by P. pastoris by approximately 97%. The genomic sequence of cel4 was isolated by screening a cosmid library of A. bisporus C54-carb8. The open reading frame was interrupted by 12 introns. The level of extracellular CEL4 increases dramatically at the postharvest stage in compost extracts of A. bisporus fruiting cultures. In laboratory liquid cultures of A. bisporus, the activity of CEL4 detected in the culture filtrate reached a maximum after 21 days. The levels of CEL4 broadly mirrored the levels of enzyme activity. In the Solka floc-bound mycelium, CEL4 protein showed a maximum after 2 to 3 weeks of culture and then declined. Changes in CEL4 activity during fruiting-body development suggest that hemicellulose utilization plays an important role in sporophore formation. The availability of the cloned gene will further studies of compost decomposition and the extracellular enzymes that fungi deploy in this process.␤-Mannanase enzymes (endo-1,4-␤-D-mannanase, mannan endo-1,4-␤-mannosidase; EC 3.2.1.78) are endohydrolases that catalyze the random hydrolysis of ␤-1,4-mannosidic linkages in the main chain of galactomannan, glucomannan, galactoglucomannan, and mannan (20). These enzymes are of particular interest in ligninolytic fungi, where there is a complex interplay between the processes of degradation of lignin, cellulose, and hemicellulose (including the mannans). There are possible biotechnological applications. ␤-Mannanase can be used to bleach pulp, to reduce the viscosity of instant coffee, and for the clarification of fruit juices and wines (35). At the same time, the role of hemicellulases in wood decay and the breakdown of leaf litter remains poorly understood. The cultivated mushroom Agaricus bisporus, a ligninolytic leaf litter degrader (8), is the source of the mannanase described in this paper.The deduced CEL4 amino acid sequence shows that the encoded protein has a modular structure (40). There is a signal peptide at the N terminus, typical of proteins that are secreted into the medium, a catalytic domain, and a linker rich in serine, proline, and threonine that separates a cellulose-binding domain from the catalytic domain. The catalytic domain of CEL4 had the most amino acid sequence similarity with ascomycete mannanases from Aspergillus aculeatus (5) and Trichoderma reesei (28), which belong to glycosyl hydrolase family 5 (43 and 42%, respectively). Therefore, based on amino acid similarities of the catalytic dom...

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An endo-1,4-β-xylanase-encoding gene from Agaricus bisporus is regulated by compost-specific factors

Cited by 34 publications

References 31 publications

Pseudomonas cellulosa expresses a single membrane-bound glycoside hydrolase family 51 arabinofuranosidase

Pseudomonas cellulosa expresses a single membrane-bound glycoside hydrolase family 51 arabinofuranosidase

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

The cel4 Gene of Agaricus bisporus Encodes a β-Mannanase

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