Molecular Biology and Evolution, Vol 15, 528-537, Copyright © 1998 by Society for Molecular Biology and Evolution
T Barbeyron, A Gerard, P Potin, B Henrissat and B Kloareg
We report here cloning from the marine gliding bacterium Cytophaga
drobachiensis of kappa-carrageenase, a glycoside hydrolase involved in the
degradation of kappa-carrageenan. Structural features in the nucleotide
sequence are pointed out, including the presence of an octameric omega
sequence similar to the ribosome-binding sites of various eukaryotes and
prokaryotes. The cgkA gene codes for a protein of 545 aa, with a signal
peptide of 35 aa and a 229-aa-long posttranslationaly processed C-terminal
domain. The enzyme displays the overall folding and catalytic domain
characteristics of family 16 of glycoside hydrolases, which comprises other
beta-1,4-alpha-1,3-D/L- galactan hydrolases, beta-1,3-D-glucan hydrolases
(laminarinases), beta- 1,4-1,3-D-glucan hydrolases (lichenases), and
beta-1,4-D-xyloglucan endotransglycosylases. In order to address the origin
and evolution of CgkA, a comprehensive phylogenetic tree of family 16 was
built using parsimony analysis. Family-16 glycoside hydrolases cluster
according to their substrate specificity, regardless of their phylogenetic
distribution over eubacteria and eukaryotes. Such a topology suggests that
the general homology between laminarinases, agarases, kappa- carrageenases,
lichenases, and xyloglucan endotransglycosylases has arisen through gene
duplication, likely from an ancestral protein with laminarinase activity.
ORIGINAL ARTICLE
The kappa-carrageenase of the marine bacterium Cytophaga drobachiensis. Structural and phylogenetic relationships within family-16 glycoside hydrolases
Centre d'Etudes d'Oceanologie et de Biologie Marine, CNRS, Roscoff, France.
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