ArticleApplied and environmental microbiology2005
Role of the bga1-encoded extracellular {beta}-galactosidase of Hypocrea jecorina in cellulase induction by lactose.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 66 citations in OpenAlex.
- Transcriptomic and metabolic changes in Trichoderma reesei caused by mutation in xylanase regulator 1 (xyr1).Biotechnology for biofuels and bioproducts · 2024Article
- Intracellular Sugar Transporters Facilitate Cellulase Synthesis inBiomolecules · 2023Article
- Article
- From induction to secretion: a complicated route for cellulase production in Trichoderma reesei.Bioresources and bioprocessing · 2021Review
- The transcription factor ACE3 controls cellulase activities and lactose metabolism via two additional regulators in the fungusThe Journal of biological chemistry · 2019Article
- Use of fusion transcription factors to reprogram cellulase transcription and enable efficient cellulase production inBiotechnology for biofuels · 2019Article
- The putative β-glucosidase BGL3I regulates cellulase induction inBiotechnology for biofuels · 2018Article
- Redesigning the regulatory pathway to enhance cellulase production in Penicillium oxalicum.Biotechnology for biofuels · 2015Article
- Intracellular β-glucosidases CEL1a and CEL1b are essential for cellulase induction on lactose in Trichoderma reesei.Eukaryotic cell · 2014Article
- Cost-effective lignocellulolytic enzyme production by Trichoderma reesei on a cane molasses medium.Biotechnology for biofuels · 2014Article
- Kinetic transcriptome analysis reveals an essentially intact induction system in a cellulase hyper-producer Trichoderma reesei strain.Biotechnology for biofuels · 2014Article
- Systems analysis of lactose metabolism in Trichoderma reesei identifies a lactose permease that is essential for cellulase induction.PloS one · 2013Article
- Re-annotation of the CAZy genes of Trichoderma reesei and transcription in the presence of lignocellulosic substrates.Microbial cell factories · 2012Article
- Function and 3D structure of the N-glycans on glycoproteins.International journal of molecular sciences · 2012Review
- Enzyme production by filamentous fungi: analysis of the secretome of Trichoderma reesei grown on unconventional carbon source.Microbial cell factories · 2011Article
- A modified expression of the major hydrolase activator inCatalysis today · 2011Article
- The effects of disruption of phosphoglucose isomerase gene on carbon utilisation and cellulase production in Trichoderma reesei Rut-C30.Microbial cell factories · 2011Article
- Differential regulation of the cellulase transcription factors XYR1, ACE2, and ACE1 in Trichoderma reesei strains producing high and low levels of cellulase.Eukaryotic cell · 2011Article
- Metabolic engineering strategies for the improvement of cellulase production by Hypocrea jecorina.Biotechnology for biofuels · 2009Article
- Crystallization and preliminary diffraction analysis of a beta-galactosidase from Trichoderma reesei.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactose is the only soluble and economically feasible carbon source for the production of cellulases or heterologous proteins regulated by cellulase expression signals by Hypocrea jecorina (Trichoderma reesei). We investigated the role of the major beta-galactosidase of H. jecorina in lactose metabolism and cellulase induction. A genomic copy of the bga1 gene was cloned, and this copy encodes a 1,023-amino-acid protein with a 20-amino-acid signal sequence. This protein has a molecular mass of 109.3 kDa, belongs to glycosyl hydrolase family 35, and is the major extracellular beta-galactosidase during growth on lactose. Its transcript was abundant during growth on l-arabinose and l-arabinitol but was much less common when the organism was grown on lactose, d-galactose, galactitol, d-xylose, and xylitol. Deltabga1 strains grow more slowly and accumulate less biomass on lactose, but the cellobiohydrolase I and II gene expression and the final cellulase yields were comparable to those of the parental strain. Overexpression of bga1 under the control of the pyruvate kinase promoter reduced the lag phase, increased growth on lactose, and limited transcription of cellobiohydrolases. We detected an additional extracellular beta-galactosidase activity that was not encoded by bga1 but no intracellular beta-galactosidase activity. In conclusion, cellulase production on lactose occurs when beta-galactosidase activity levels are low but decreases as the beta-galactosidase activities increase. The data indicate that bga1-encoded beta-galactosidase activity is a critical factor for cellulase production on lactose.
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