CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.
Thurston, Christopher F. Yague, Ernesto
Thurston, Christopher F.
Yague, Ernesto
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Epub Date
Issue Date
1994
Submitted date
2007-01-24
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Abstract
The 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.
Citation
FEMS Microbiology Letters, 116(3): 293-299
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Research Unit
PubMed ID
8181702
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Journal article
Language
en
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ISSN
0378-1097