Armesilla, AngelThurston, Christopher F.Yague, Ernesto2007-01-242007-01-2419942007-01-24FEMS Microbiology Letters, 116(3): 293-2990378-1097818170210.1111/j.1574-6968.1994.tb06718.xhttp://hdl.handle.net/2436/7745Metadata onlyThe 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.enAgaricus bisporusCEL1CelluloseProteinsJournal articleYES