ArticleBiotechnology for biofuels2021
Carbon catabolite repression involves physical interaction of the transcription factor CRE1/CreA and the Tup1-Cyc8 complex in Penicillium oxalicum and Trichoderma reesei.
Article in Biotechnology for biofuels, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 26 citations in OpenAlex.
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- Advancing cellulose degradation through synthetic biology: engineered pathways and microbial systems for sustainable biomass conversion.Journal of animal science and biotechnology · 2026Review
- The Transcription Factor PoCon7 Is Essential for Fungal Viability and Regulates Chitinase Gene Expression inInternational journal of molecular sciences · 2025Article
- Rme1: Unveiling a Novel Repressor in the Cellulolytic Pathway ofJournal of fungi (Basel, Switzerland) · 2025Article
- Biodegradation of screenings from sewage treatment by white rot fungi.Fungal biology and biotechnology · 2025Article
- Discovery of a novel translation-machinery-associated protein that positively correlates with cellulase production.Biotechnology for biofuels and bioproducts · 2025Article
- F-box protein Fbx23 acts as a transcriptional coactivator to recognize and activate transcription factor Ace1.PLoS genetics · 2025Article
- Regulation of genes encoding polysaccharide-degrading enzymes in Penicillium.Applied microbiology and biotechnology · 2024Review
- Calcium signaling positively regulates cellulase translation and secretion in a Clr-2-overexpressing, catabolically derepressed strain of Penicillium funiculosum.Biotechnology for biofuels and bioproducts · 2024Article
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Abstract
backgroundCellulolytic enzyme production in filamentous fungi requires a release from carbon catabolite repression (CCR). The protein CRE1/CreA (CRE = catabolite responsive element) is a key transcription factor (TF) that is involved in CCR and represses cellulolytic gene expression. CRE1/CreA represents the functional equivalent of Mig1p, an important Saccharomyces cerevisiae TF in CCR that exerts its repressive effect by recruiting a corepressor complex Tup1p-Cyc8p. Although it is known from S. cerevisiae that CRE1/CreA might repress gene expression via interacting with the corepressor complex Tup1-Cyc8, this mechanism is unconfirmed in other filamentous fungi, since the physical interaction has not yet been verified in these organisms. The precise mechanism on how CRE1/CreA achieves transcriptional repression after DNA binding remains unknown.
resultsThe results from tandem affinity purification and bimolecular fluorescence complementation revealed a direct physical interaction between the TF CRE1/CreA and the complex Tup1-Cyc8 in the nucleus of cellulolytic fungus Trichoderma reesei and Penicillium oxalicum. Both fungi have the ability to secrete a complex arsenal of enzymes to synergistically degrade lignocellulosic materials. In P. oxalicum, the protein PoCyc8, a subunit of complex Tup1-Cyc8, interacts directly with TF PoCreA and histone H3 lysine 36 (H3K36) methyltransferase PoSet2 in the nucleus. The di-methylation level of H3K36 in the promoter of prominent cellulolytic genes (cellobiohydrolase-encoding gene Pocbh1/cel7A and endoglucanase-encoding gene Poegl1/cel7B) is positively correlated with the expression levels of TF PoCreA. Since the methylation of H3K36 was also demonstrated to be a repression marker of cellulolytic gene expression, it appears feasible that the cellulolytic genes are repressed via PoCreA-Tup1-Cyc8-Set2-mediated transcriptional repression.
conclusionThis study verifies the long-standing conjecture that the TF CRE1/CreA represses gene expression by interacting with the corepressor complex Tup1-Cyc8 in filamentous fungi. A reasonable explanation is proposed that PoCreA represses gene expression by recruiting complex PoTup1-Cyc8. Histone methyltransferase Set2, which methylates H3K36, is also involved in the regulatory network by interacting with PoCyc8. The findings contribute to the understanding of CCR mechanism in filamentous fungi and could aid in biotechnologically relevant enzyme production.
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