AoXlnR was isolated as a transcriptional activator of the major xylanase gene, xynF1, in Aspergillus oryzae. To investigate the spectrum of genes under the control of AoXlnR, expression of the xylanolytic and cellulolytic genes in an A. oryzae wild type strain, an AoxlnR disruptant and an AoXlnR overexpressed strain was analyzed by Northern blotting. AoXlnR mediated expression of at least four xylanolytic genes and four cellulolytic genes when induced by xylan and D-xylose. Moreover, AoXlnR was newly found to mediate the cellulose-inductive expression of the xylanolytic genes as well as the cellulolytic genes.
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http://dx.doi.org/10.1016/s0014-5793(02)03328-8 | DOI Listing |
Int J Biol Macromol
November 2024
Department of Biochemistry and Immunology, Faculty of Medicine of Ribeirão Preto, University of São Paulo, Ribeirão Preto 14049-900, SP, Brazil; Department of Biology, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto 14040-901, SP, Brazil. Electronic address:
Acetylxylan esterases (AXEs) are essential enzymes that break down the acetyl groups in acetylated xylan found in plant cell walls polysaccharides. They work synergistically with backbone-depolymerizing xylanolytic enzymes to accelerate the degradation of complex polysaccharides. In this study, we cloned the gene axeA, which encodes the acetylxylan esterase from Aspergillus nidulans FGSC A4 (AxeAN), into the pEXPYR expression vector and introduced it into the high protein-producing strain A.
View Article and Find Full Text PDFNat Commun
September 2024
Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
This study introduces a synthetic biology approach that reprograms the yeast mating-type switching mechanism for tunable cell differentiation, facilitating synthetic microbial consortia formation and cooperativity. The underlying mechanism was engineered into a genetic logic gate capable of inducing asymmetric sexual differentiation within a haploid yeast population, resulting in a consortium characterized by mating-type heterogeneity and tunable population composition. The utility of this approach in microbial consortia cooperativity was demonstrated through the sequential conversion of xylan into xylose, employing haploids of opposite mating types each expressing a different enzyme of the xylanolytic pathway.
View Article and Find Full Text PDFInt J Biol Macromol
June 2024
Biochemistry Laboratory, Department of Analytical and Food Chemistry, University of Vigo, Ourense, Spain. Electronic address:
Several fungal species produce diverse carbohydrate-active enzymes useful for the xylooligosaccharide biorefinery. These enzymes can be isolated by different purification methods, but fungi usually produce other several compounds which interfere in the purification process. So, the present work has three interconnected aims: (i) compare β-xylosidase production by Fusarium pernambucanum MUM 18.
View Article and Find Full Text PDFEnviron Microbiol Rep
April 2024
Extreme Microbiology, Biotechnology and Astrobiology Group, Institute of Polar Sciences, ISP-CNR, Messina, Italy.
DNA methylation serves a variety of functions across all life domains. In this study, we investigated archaeal methylomics within a tripartite xylanolytic halophilic consortium. This consortium includes Haloferax lucertense SVX82, Halorhabdus sp.
View Article and Find Full Text PDFPhytopathology
July 2024
Hubei Key Laboratory of Plant Pathology, College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
Transcription factors play critical roles in diverse biological processes in fungi. XlnR, identified as a transcriptional activator that regulates the expression of the extracellular xylanase genes in fungi, has not been extensively studied for its function in fungal development and pathogenicity in rice false smut fungus . In this study, we characterized in and established that the full-length, N-terminal, and C-terminal forms have the ability to activate transcription.
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