Cellulase secretion from a hyper-cellulolytic mutant of Trichoderma reesei Rut-C30

Ghosh, Arati; Ghosh, B. K.; Trimiño-Vazquez, H.; Eveleigh, D. E.; Montenecourt, Bland S.

doi:10.1007/bf00454914

Cited by 49 publications

(11 citation statements)

References 28 publications

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“…It should be noted that T. reesei RUT C-30 has not been selected for carbon catabolite repression only, but primarily for increased cellulase overproduction (Montenecourt and Eveleigh, 1979), and probably harbours other mutations as well (such as in the early steps of the secretory pathway, cf. Ghosh et a/., 1984); thus, the relationship of Crel to the high basal level of transcription and the increase in induction in this strain must be interpreted with caution. However, the occurence of basal transcription and the inducibility beyond this level is in accordance with the model of Crel repression of xynl expression developed in this study.…”

Section: Discussionmentioning

confidence: 93%

Carbon catabolite repression of xylanase I (xyn1) gene expression in Trichoderma reesei

Mach

Strauss

Zeilinger

et al. 1996

Molecular Microbiology

170

167

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The filamentous fungus Trichoderma reesei forms two specific, xylan-inducible xylanases encoded by xyn1 and xyn2 to degrade the beta-1,4-D-xylan backbone of hemicelluloses. This enzyme system is formed in the presence of xylan, but not glucose. The molecular basis of the absence of xylanase I formation on glucose was the purpose of this study. Northern blotting of the xyn1 transcript as well as the use of the Escherichia coli hygromycin B phosphotransferase-encoding gene (hph) as a reporter consistently showed that the basal expression of xyn1 was affected by glucose, whereas its induction by xylan remained uninfluenced. The repression of basal xyn1 transcription is mediated by the carbon catabolite repressor protein Cre1, which in vivo binds to two of four consensus sites (5'-SYG-GRG-3') in the xyn1 promoter, which occurred in the form of an inverted repeat. T. reesei strains, bearing a xyn1::hph reporter construct, in which four nucleotides from the middle of the inverted repeat had been removed, expressed hph on glucose at a level comparable to that observed during growth on a carbon catabolite derepressing carbon source. Northern analysis of xyn1 expression in a T. reesei mutant strain (RUT C-30), which contains a truncated, non-functional cre1 gene, also confirmed basal transcription of xyn1. In this strain, xyn1 transcription was still inducible by xylose or xylan to an even higher degree than in the wild-type strain, suggesting that induction overcomes glucose repression at the level of xyn1 expression. Based on these data, we postulate that basal transcription of xyn1 is repressed by glucose and mediated by an inverted repeat of the consensus motif for Cre1-mediated carbon catabolite repression.

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Section: Discussionmentioning

confidence: 93%

Carbon catabolite repression of xylanase I (xyn1) gene expression in Trichoderma reesei

Mach

Strauss

Zeilinger

et al. 1996

Molecular Microbiology

170

167

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“…It has been reported that the proliferation of rough ER in T. reesei hyper-cellulolytic mutants was accompanied by an increased secretion of cellulase. 111) In addition to ER, vacuoles of differing sizes were observed to be randomly distributed in the cytoplasm of large numbers of cells in both strains. PC-3-7, in particular, had many vacuoles that were much larger than those of QM9414 ( Fig.…”

Section: Morphological Analysis Of T Reeseimentioning

confidence: 94%

Deciphering the molecular mechanisms behind cellulase production in Trichoderma reesei, the hyper-cellulolytic filamentous fungus

Shida

Furukawa

Ogasawara

2016

Bioscience, Biotechnology, and Biochemistry

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The filamentous fungus Trichoderma reesei is a potent cellulase producer and the best-studied cellulolytic fungus. A lot of investigations not only on glycoside hydrolases produced by T. reesei, but also on the machinery controlling gene expression of these enzyme have made this fungus a model organism for cellulolytic fungi. We have investigated the T. reesei strain including mutants developed in Japan in detail to understand the molecular mechanisms that control the cellulase gene expression, the biochemical and morphological aspects that could favor this phenotype, and have attempted to generate novel strains that may be appropriate for industrial use. Subsequently, we developed recombinant strains by combination of these insights and the heterologous-efficient saccharifing enzymes. Resulting enzyme preparations were highly effective for saccharification of various biomass. In this review, we present some of the salient findings from the recent biochemical, morphological, and molecular analyses of this remarkable cellulase hyper-producing fungus.

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“…In analogy, the present results might be summarized as stimulation of protein secretion by fatty acids. Ghosh and coworkers have stressed that protein secretion in T. reesei is limited by the amount of endoplasmic reticulum [26]. It is tempting to speculate whether low producer strains of Trichoderma are limited in their secretory capacity at the level of membrane biogenesis, which can be relieved by supplementation of lipid precursors.…”

Section: Discussionmentioning

confidence: 99%

Stimulation of protein secretion in Trichoderma reesei by Tween surfactants is not correlated with changes in enzyme localization or membrane fatty acid composition

Panda

1987

FEMS Microbiology Letters

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Cellulase secretion from a hyper-cellulolytic mutant of Trichoderma reesei Rut-C30

Cited by 49 publications

References 28 publications

Carbon catabolite repression of xylanase I (xyn1) gene expression in Trichoderma reesei

Carbon catabolite repression of xylanase I (xyn1) gene expression in Trichoderma reesei

Deciphering the molecular mechanisms behind cellulase production in Trichoderma reesei, the hyper-cellulolytic filamentous fungus

Stimulation of protein secretion in Trichoderma reesei by Tween surfactants is not correlated with changes in enzyme localization or membrane fatty acid composition

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