CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.

2.50
Hdl Handle:
http://hdl.handle.net/2436/7745
Title:
CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.
Authors:
Armesilla, Angel Luis; Thurston, Christopher F.; Yague, Ernesto
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
Publisher:
Blackwell Publishing
Issue Date:
1994
URI:
http://hdl.handle.net/2436/7745
DOI:
10.1111/j.1574-6968.1994.tb06718.x
PubMed ID:
8181702
Additional Links:
http://www3.interscience.wiley.com/journal/119276698/abstract
Submitted date:
2007-01-24
Type:
Article
Language:
en
Description:
Metadata only
ISSN:
0378-1097
Appears in Collections:
Molecular Pharmacology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorArmesilla, Angel Luis-
dc.contributor.authorThurston, Christopher F.-
dc.contributor.authorYague, Ernesto-
dc.date.accessioned2007-01-24T14:42:50Z-
dc.date.available2007-01-24T14:42:50Z-
dc.date.issued1994-
dc.date.submitted2007-01-24-
dc.identifier.citationFEMS Microbiology Letters, 116(3): 293-299en
dc.identifier.issn0378-1097-
dc.identifier.pmid8181702-
dc.identifier.doi10.1111/j.1574-6968.1994.tb06718.x-
dc.identifier.urihttp://hdl.handle.net/2436/7745-
dc.descriptionMetadata onlyen
dc.description.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.en
dc.language.isoenen
dc.publisherBlackwell Publishingen
dc.relation.urlhttp://www3.interscience.wiley.com/journal/119276698/abstract-
dc.subjectAgaricus bisporusen
dc.subjectCEL1en
dc.subjectCelluloseen
dc.subjectProteinsen
dc.titleCEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.en
dc.typeArticleen
dc.format.digYES-
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