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Glycobiology Advance Access published online on July 31, 2006
Glycobiology, doi:10.1093/glycob/cwl029
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received December 5, 2005
Revised June 23, 2006
Accepted July 18, 2006

Article

Cloning and biochemical characterization of the fucanase FcnA: definition of a novel glycoside hydrolase family specific for sulfated fucans

Sébastien Colin 1, Estelle Deniaud 1, Murielle Jam 1, Valérie Descamps 1, Yann Chevolot 1, Nelly Kervarec 2, Jean-Claude Yvin 3, Tristan Barbeyron 1, Gurvan Michel 1 *, and Bernard Kloareg 1

1 Equipe Glycobiologie Marine, Centre National de la Recherche Scientifique; Université Pierre et Marie Curie-Paris6, Unité Mixte de Recherche 7139, Station Biologique, F-29682 Roscoff Cedex, Bretagne, France
2 Service Commun de Résonance Magnétique Nucléaire, Université de Bretagne Occidentale, Brest, Bretagne, France
3 Laboratoires Goëmar, Saint Malo, Bretagne, France

* To whom correspondence should be addressed.
Gurvan Michel, E-mail: gurvan{at}sb-roscoff.fr


  Abstract

Sulfated fucans are matrix polysaccharides from marine brown algae, consisting of a {alpha}L-fucose backbone substituted by sulfate-ester groups, masked with ramifications, and containing other monosaccharide residues. We here report on the characterization of a novel glycoside hydrolase (FcnA), specific for the degradation of sulfated fucans. This glycoside hydrolase was purified to electrophoretic homogeneity from a Flavobacteriaceae referred to as SW5. The gene fcnA was cloned and sequenced (3021 nucleotides) and the protein (1007 amino acids) was produced in E. coli. FcnA exhibited a modular architecture, consisting of a 400 residues - long N-terminal domain followed by three repeated domains predicted to adopt an immunoglobulin fold and by a 80 amino acids - long C-terminal domain. A truncated recombinant protein encompassing the N-terminal domain and the immunoglobulin-like repeats was shown to retain the enzyme activity. The N-terminal catalytic domain shared about 25% of sequence identity with two patented fucanase genes and these three fucanases delineate a new family of glycoside hydrolases. As shown by size exclusion chromatography and 1H-NMR analyses, the fucanase FcnA proceeds according an endo mode of action and cleaves the {alpha}-(1->4) glycosidic linkages within blocks of repeating motifs [->4)-{alpha}-L-fucopyranosyl-2,3-disulfate-(1->3)-{alpha}-L-fucopyranosyl-2-sulfate-(1->]n.

Keywords: fucanase, sulfated polysaccharide, Flavobacteriaceae, brown algae, NMR.
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