Cloning and targeted disruption of MLG1, a gene encoding two of three extracellular mixed-linked glucanases of Cochliobolus carbonum
Article Abstract:
Mixed-linked glucanases (MLGases) or extracellular enzymes that degrade beta-glucan from the fungus Cochliobolus carbonum were identified and characterized. Three peaks of MLGase activity, named Mlg1a, Mlg1b and Mlg2, were resolved by hydrophobic-interaction high performance liquid chromatography and cation-exchange. Results showed that the N-terminal amino acid sequences of Mlg1a and Mlg1b were identical. Mlg1a was glycosylated while Mlg1b was not. Mlg1a and Mlg1b hydrolyzed beta1,3-glucan while Mlg2 did not.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
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Cloning, disruption, and expression of two endo-beta-1,4-xylanase genes, XYL2 and XYL3, from Cochliobolus carbonum
Article Abstract:
The filamentous fungi Cochliobolus carbonum contains three cationic xylanases, XYL1, XYL2 and XYL3 that encode for the extracellular 22-kDa family of G xylanases. XYL1 and XYL3 mRNA's are present in infected plants. XYL2 and XYL3 have no contribution towards the extracellular xylanase activity. Multiple xylanase disruptions are produced by crossing single xylanase mutants. The triple mutant is still pathogenic on maize as evident from its lesion size, morphology and rate of lesion development.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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A unique eukaryotic beta-xylosidase gene from the phytopathogenic fungus Cochliobolus carbonum
Article Abstract:
A study was conducted to analyze a novel eukaryotic beta-xylosidase (Xyp1) gene from the phytopathogenic fungus Cochliobolus carbonum. cDNA and genomic DNA encoding Xyp1 were determined using polymerase chain reaction primers based on peptide sequences from the purified protein. Results indicated that the mutation of the XYP1 by targeted gene replacement led to the loss of the major beta-xylosidase activity correlated with the product of XYP1.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1999
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