Expression of CEL2 and CEL4, two proteins from Agaricus bisporus with similarity to fungal cellobiohydrolase I and beta-mannanase, respectively, is regulated by the carbon source
Article Abstract:
Recombinant DNA techniques were used for the isolation and characterization of two new Agaricus bisporus cellulose-growth specific (cel) cDNAs designated cel2 and cel4. Amino acid sequence analysis showed that the CEL2 and CEL4 proteins have a modular structure composed of a fungal-type cellulose-binding domain and a catalytic domain separated by a linker region rich in Pro, Ser and Thr. The latter domain was found to be homologous to fungal cellobiohydrolases in family 7 (CEL4) and to fungal mannanases in family 5 (CEL4) of the glycosyl hydrolases. The expression of the two genes was demonstrated by RNA analysis to be enhanced by cellulose and inhibited by glucose, fructose and lactose.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Enzymic activity of the mycoparasite Verticillium fungicola on Agaricus bisporus fruit body cell walls
Article Abstract:
A study was conducted on the enzymic activity of the mycoparasite Verticillium fungicola on Agaricus bisporus fruit bodies. The Verticillium fungicola was grown with several carbon sources, including glucose, fructose, surcose and Agaricus bisporus cell walls. Results have shown that The enzyme activities produced by Verticillium fungicola on Agaricus bisporus walls are greater than those in the three other sources.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Purification of geranylgeranyltransferase I from Candida albicans and cloning of the CaRAM2 and CaCDC43 genes encoding its subunits
Article Abstract:
A study was conducted to analyze the function of geranylgeranylation in the pathogenic yeast, Candida albicans. GGTase I was purified to near homogeneity. An acid quench-filtration assay was utilized to determine protein prenyltransferase activities. Results indicated that GGTase I was a heterodimeric magnesium-dependent, zinc metalloenzyme supporting selectivity for CaaL-containing protein substrates.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1999
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