Regulation of pentose utilisation by AraR, but not XlnR, differs in Aspergillus nidulans and Aspergillus niger
Open Access
- 12 April 2011
- journal article
- applied microbial-and-cell-physiology
- Published by Springer Nature in Applied Microbiology and Biotechnology
- Vol. 91 (2) , 387-397
Abstract
Filamentous fungi are important producers of plant polysaccharide degrading enzymes that are used in many industrial applications. These enzymes are produced by the fungus to liberate monomeric sugars that are used as carbon source. Two of the main components of plant polysaccharides are l-arabinose and d-xylose, which are metabolized through the pentose catabolic pathway (PCP) in these fungi. In Aspergillus niger, the regulation of pentose release from polysaccharides and the PCP involves the transcriptional activators AraR and XlnR, which are also present in other Aspergilli such as Aspergillus nidulans. The comparative analysis revealed that the regulation of the PCP by AraR differs in A. nidulans and A. niger, whereas the regulation of the PCP by XlnR was similar in both species. This was demonstrated by the growth differences on l-arabinose between disruptant strains for araR and xlnR in A. nidulans and A. niger. In addition, the expression profiles of genes encoding l-arabinose reductase (larA), l-arabitol dehydrogenase (ladA) and xylitol dehydrogenase (xdhA) differed in these strains. This data suggests evolutionary changes in these two species that affect pentose utilisation. This study also implies that manipulating regulatory systems to improve the production of polysaccharide degrading enzymes, may give different results in different industrial fungi.Keywords
This publication has 28 references indexed in Scilit:
- Analysis of regulation of pentose utilisation in Aspergillus niger reveals evolutionary adaptations in EurotialesStudies in Mycology, 2011
- The ‘true’ l‐xylulose reductase of filamentous fungi identified in Aspergillus nigerFEBS Letters, 2010
- Identification of an l-Arabinose Reductase Gene in Aspergillus niger and Its Role in l-Arabinose CatabolismJournal of Biological Chemistry, 2010
- Identification and Characterization of l-Arabonate Dehydratase, l-2-Keto-3-deoxyarabonate Dehydratase, and l-Arabinolactonase Involved in an Alternative Pathway of l-Arabinose MetabolismJournal of Biological Chemistry, 2006
- Cloning, Expression, and Characterization of Bacterial l-Arabinose 1-Dehydrogenase Involved in an Alternative Pathway of l-Arabinose MetabolismJournal of Biological Chemistry, 2006
- A New Black Aspergillus Species, A. vadensis , Is a Promising Host for Homologous and Heterologous Protein ProductionApplied and Environmental Microbiology, 2004
- Multiple sequence alignment with the Clustal series of programsNucleic Acids Research, 2003
- Characterization of an -arabitol dehydrogenase mutantFEMS Microbiology Letters, 1994
- Characterization of anAspergillus nidulansL-arabitol dehydrogenase mutantFEMS Microbiology Letters, 1994
- L-Arabinose and D-Xylose Catabolism in Aspergillus nigerMicrobiology, 1989