Functional Analysis of an Endo-1,6-β-<scp>D</scp>-glucanase Gene (<i>neg-1</i>) from<i>Neurospora crassa</i>

Oyama, Seiji; Inoue, Hirokazu; Yamagata, Yuriko; Nakajima, Tasuku; Abe, Keietu

doi:10.1271/bbb.50626

Cited by 7 publications

(7 citation statements)

References 12 publications

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“…Overall, 22 proteins identified in the pectin secretome overlapped with the xylan secretome, versus only 12 proteins that overlapped with the Avicel secretome. Of the nine proteins in common between all three secretomes, six are associated with the N. crassa cell wall and/or implicated in cell wall remodelling: NEG‐1/NCU04395, NCW‐1/NCU05137, Mwg1/NCU05974, ACW‐12/NCU08171, ACW‐1/NCU08936, and EglC/NCU09175 (Oyama et al ., ; Maddi et al ., ). In addition, one endo‐xylanase (GH10‐2/NCU08189) and two proteins of unknown function were detected (NCU00798 and NCU09024).…”

Section: Resultsmentioning

confidence: 98%

A comparative systems analysis of polysaccharide‐elicited responses in Neurospora crassa reveals carbon source‐specific cellular adaptations

Benz

Chau

Zheng

et al. 2013

Molecular Microbiology

100

141

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Summary Filamentous fungi are powerful producers of hydrolytic enzymes for the deconstruction of plant cell wall polysaccharides. However, the central question of how these sugars are perceived in the context of the complex cell wall matrix remains largely elusive. To address this question in a systematic fashion we performed an extensive comparative systems analysis of how the model filamentous fungus Neurospora crassa responds to the three main cell wall polysaccharides: pectin, hemicellulose and cellulose. We found the pectic response to be largely independent of the cellulolytic one with some overlap to hemicellulose, and in its extent surprisingly high, suggesting advantages for the fungus beyond being a mere carbon source. Our approach furthermore allowed us to identify carbon source-specific adaptations, such as the induction of the unfolded protein response on cellulose, and a commonly induced set of 29 genes likely involved in carbon scouting. Moreover, by hierarchical clustering we generated a co-expression matrix useful for the discovery of new components involved in polysaccharide utilization. This is exemplified by the identification of lat-1, which we demonstrate to encode for the physiologically relevant arabinose transporter in Neurospora. The analyses presented here are an important step towards understanding fungal degradation processes of complex biomass.

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Section: Resultsmentioning

confidence: 98%

A comparative systems analysis of polysaccharide‐elicited responses in Neurospora crassa reveals carbon source‐specific cellular adaptations

Benz

Chau

Zheng

et al. 2013

Molecular Microbiology

100

141

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“…The chemical characteristics of saponins may be considered analogous to glucosylceramides, both having glycosyl moieties O‐linked to large hydrophobic molecules. A clear distinction is observed between these β‐glucosidase/β‐xylosidase like enzymes that have exo‐function and the phylogenetically related endo‐β‐1,6‐glucanase [17,18]. These later enzymes function in an endo‐manner and have been characterized to degrade β‐1,6‐glucan, a polysaccharide component of fungal cell walls [19,20].…”

Section: Introductionmentioning

confidence: 99%

Consolidation of glycosyl hydrolase family 30: A dual domain 4/7 hydrolase family consisting of two structurally distinct groups

2010

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Keywords:Glycosyl hydrolase family 30 (GH30) Glycosyl hydrolase family 5 (GH5) Glucuronoxylan xylanohydrolase Endo-b-1,6-galactanase Glucosylceramidase Endo-b-1,6-glucanase a b s t r a c tIn this work glycosyl hydrolase (GH) family 30 (GH30) is analyzed and shown to consist of its currently classified member sequences as well as several homologous sequence groups currently assigned within family GH5. A large scale amino acid sequence alignment and a phylogenetic tree were generated and GH30 groups and subgroups were designated. A partial rearrangement in the GH30 defining side-associated b-domain contributes to the differentiation of two major groups that contain up to eight subgroups. For this CAZy family of Clan A enzymes the dual domain fold is conserved, suggesting that it may be a requirement for evolved function. This work redefines GH family 30 and serves as a guide for future efforts regarding enzymes classified within this family.Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

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“…The lack of diVerences between wild type, gcnA deletion and overexpressing strains when grown under conditions aVecting cell wall structure suggested that loss or overexpression of GcnA did not aVect -glucan structure in the cell wall. These results diVer from those found for the Neg1 -1,6-glucanase from glycosyl hydrolase family 30 in N. crassa, where disruption of neg1 gene resulted in increased sensitivity to the cell walldestabilising agents Congo Red and sodium dodecyl sulfate (Oyama et al, 2006). Due to the nature of -1,6-glucans as cross-linking agents within the wall, it has been suggested -1,6-glucanases may play a role in hyphal branching (Moy et al, 2002).…”

Section: Discussionmentioning

confidence: 71%

Functional analysis of a β-1,6-glucanase gene from the grass endophytic fungus Epichloë festucae

Bryant

May

Bryan

et al. 2007

Fungal Genetics and Biology

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Functional Analysis of an Endo-1,6-β-D-glucanase Gene (neg-1) fromNeurospora crassa

Cited by 7 publications

References 12 publications

A comparative systems analysis of polysaccharide‐elicited responses in Neurospora crassa reveals carbon source‐specific cellular adaptations

A comparative systems analysis of polysaccharide‐elicited responses in Neurospora crassa reveals carbon source‐specific cellular adaptations

Consolidation of glycosyl hydrolase family 30: A dual domain 4/7 hydrolase family consisting of two structurally distinct groups

Functional analysis of a β-1,6-glucanase gene from the grass endophytic fungus Epichloë festucae

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