Carbon repression of cellobiose dehydrogenase production in the white rot fungus<i>Trametes versicolor</i>is mediated at the level of gene transcription

Stapleton, Patricia; Dobson, Alan D. W.

doi:10.1016/s0378-1097(03)00212-x

Cited by 24 publications

(12 citation statements)

References 30 publications

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“…As postulated for cellulases and hemicellulases, the absence of CDH could be explained by the presence of traces of glucose, since the expression of the T. versicolor orthologue is also strongly regulated at transcriptional level by carbon catabolite repression mechanisms [67].…”

Section: Resultsmentioning

confidence: 92%

A First Insight into Pycnoporus sanguineus BAFC 2126 Transcriptome

et al. 2013

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Fungi of the genus Pycnoporus are white-rot basidiomycetes widely studied because of their ability to synthesize high added-value compounds and enzymes of industrial interest. Here we report the sequencing, assembly and analysis of the transcriptome of Pycnoporus sanguineus BAFC 2126 grown at stationary phase, in media supplemented with copper sulfate. Using the 454 pyrosequencing platform we obtained a total of 226,336 reads (88,779,843 bases) that were filtered and de novo assembled to generate a reference transcriptome of 7,303 transcripts. Putative functions were assigned for 4,732 transcripts by searching similarities of six-frame translated sequences against a customized protein database and by the presence of conserved protein domains. Through the analysis of translated sequences we identified transcripts encoding 178 putative carbohydrate active enzymes, including representatives of 15 families with roles in lignocellulose degradation. Furthermore, we found many transcripts encoding enzymes related to lignin hydrolysis and modification, including laccases and peroxidases, as well as GMC oxidoreductases, copper radical oxidases and other enzymes involved in the generation of extracellular hydrogen peroxide and iron homeostasis. Finally, we identified the transcripts encoding all of the enzymes involved in terpenoid backbone biosynthesis pathway, various terpene synthases related to the biosynthesis of sesquiterpenoids and triterpenoids precursors, and also cytochrome P450 monooxygenases, glutathione S-transferases and epoxide hydrolases with potential functions in the biodegradation of xenobiotics and the enantioselective biosynthesis of biologically active drugs. To our knowledge this is the first report of a transcriptome of genus Pycnoporus and a resource for future molecular studies in P. sanguineus.

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Section: Resultsmentioning

confidence: 92%

A First Insight into Pycnoporus sanguineus BAFC 2126 Transcriptome

et al. 2013

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“…The repression of CDH biosynthesis both by glucose and by the disaccharide maltose is mediated at the level of transcription. A number of putative Cre-A or Cre1 repressor-like binding sites were detected in a 1.6-kb upstream region of the T. versicolor cdh gene [31]. These sites displayed high sequence similarity with consensus sites for binding repressor proteins in Aspergillus and Trichoderma species, and it was concluded that these sites might be responsible for the repressive effect on cdh transcription.…”

Section: Production Of Cdh In Basidiomycetesmentioning

confidence: 96%

“…Further, it was shown that CDH production in both Grifola frondosa [30] and T. versicolor [31] is subject to carbon catabolite repression. Such metabolic regulation is interpreted as an energy-saving response whereby readily metabolisable carbohydrates, such as glucose, repress the synthesis of enzymes involved in the catabolism of alternative carbon sources.…”

Section: Production Of Cdh In Basidiomycetesmentioning

confidence: 99%

Cellobiose Dehydrogenase – A Flavocytochrome from Wood-Degrading, Phytopathogenic and Saprotropic Fungi

Zámocký¹,

Ludwig

Peterbauer

et al. 2006

CPPS

221

230

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Cellobiose dehydrogenase, the only currently known extracellular flavocytochrome, is formed not only by a number of wood-degrading but also by various phytopathogenic fungi. This inducible enzyme participates in early events of lignocellulose degradation, as investigated in several basidiomycete fungi at the transcriptional and translational level. However, its role in the ascomycete fungi is not yet obvious. Comprehensive sequence analysis of CDH-encoding genes and their translational products reveals significant sequence similarities along the entire sequences and also a common domain architecture. All known cellobiose dehydrogenases fall into two related subgroups. Class-I members are represented by sequences from basidiomycetes whereas class-II comprises longer, more complex sequences from ascomycete fungi. Cellobiose dehydrogenase is typically a monomeric protein consisting of two domains joined by a protease-sensitive linker region. Each larger (dehydrogenase) domain is flavin-associated while the smaller (cytochrome) domains are haem-binding. The latter shorter domains are unique sequence motifs for all currently known flavocytochromes. Each cytochrome domain of CDH can bind a single haem b as prosthetic group. The larger dehydrogenase domain belongs to the glucose-methanol-choline (GMC) oxidoreductase superfamily - a widespread flavoprotein evolutionary line. The larger domains can be further divided into a flavin-binding subdomain and a substrate-binding subdomain. In addition, the class-II (but not class-I) proteins can possess a short cellulose-binding module of type 1 at their C-termini. All the cellobiose dehydrogenases oxidise cellobiose, cellodextrins, and lactose to the corresponding lactones using a wide spectrum of different electron acceptors. Their flexible specificity serves as a base for the development of possible biotechnological applications.

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“…1A in the glucose cultures laccase activity first appeared on day 4 (372 U/l) and then it sharply increased to 4304 U/l on day 7 reaching its peak on the last cultivation day (7974 U/l). CDH was not detected, since glucose inhibits CDH expression [21]. As for cellulose cultures (Fig.…”

Section: Enzyme Productionmentioning

confidence: 86%