CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.
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AbstractThe cel1 gene of Agaricus bisporus encodes a protein (CEL1) that has an architecture resembling the multi-domain fungal cellulases, although the sequence of its putative catalytic core is not matched by any other in the protein and nucleic acid data bases. The N-terminal half of the putative catalytic domain of CEL1 was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase. The fusion protein was used to raise a CEL1-specific antibody. CEL1 was detected as an extracellular 49.8 kDa protein in A. bisporus cellulose-grown cultures, where it bound strongly to cellulose. CEL1 was neither an endoglucanase, a cellobiohydrolase able to hydrolyze fluorogenic cellobiosides, a beta-glucosidase, a xylanase, nor a cellobiose: quinone oxidoreductase. CEL1 was present in some fractions of culture fluid separated by electrophoresis which released soluble sugars from crystalline cellulose.
CitationFEMS Microbiology Letters, 116(3): 293-299
- Isolation and characterization of a cellulose-growth-specific gene from Agaricus bisporus.
- Authors: Raguz S, Yagüe E, Wood DA, Thurston CF
- Issue date: 1992 Oct 1
- Regulation of transcription of the cel1 gene in Agaricus bisporus.
- Authors: Yagüe E, Wood DA, Thurston CF
- Issue date: 1994 Apr
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- Authors: Morales P, Thurston CF
- Issue date: 2003 Apr
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- Authors: Yage E, Mehak-Zunic M, Morgan L, Wood DA, Thurston CF
- Issue date: 1997 Jan
- Characterization and disruption of a gene in the maize pathogen Cochliobolus carbonum encoding a cellulase lacking a cellulose binding domain and hinge region.
- Authors: Sposato P, Ahn JH, Walton JD
- Issue date: 1995 Jul-Aug