@article{3714,
  keywords = {Animals, Crassostrea, Phylogeny, Species Specificity, Protein Conformation, Gene Expression Regulation, Enzymologic, Glycoside Hydrolases},
  author = {Fabien Badariotti and Christophe Lelong and Marie-Pierre Dubos and Pascal Favrel},
  title = {Identification of three singular glycosyl hydrolase family 18 members from the oyster Crassostrea gigas: Structural characterization, phylogenetic analysis and gene expression.},
  abstract = {<p>Glycoside hydrolase family 18 (GH18) includes chitinases and non-enzymatic chitinase-like proteins (CLPs) with representatives among eukaryotes (animals and plants), prokaryotes and viruses. In Lophotrochozoa, one of the three clades of bilaterian animals, only three members (Cg-Clp1, Cg-Clp2 and Cg-Chit) have been reported from the bivalve mollusc Crassostrea gigas. Here, we describe the cloning and the characterization of two additional chitinases (Cg-Chit2 and Cg-Chit3) and a new CLP (Cg-Clp3) from this species. Cg-Chit2 presents an atypical C-terminal hydrophobic region acting probably as a GPI-anchor signal for plasma membrane attachment. On the contrary, Cg-Chit3 displays a C-terminal truncated structure leading to a possible sequestration in lysosomes. Phylogenetic analyses suggest that CLPs have appeared independently in the three main branches of bilaterian animals, as a result of convergent evolution. Gene expression profiles analyzed by quantitative RT-PCR support the involvement of Cg-Clp3 in embryonic development, adult oyster growth and tissue remodelling during metamorphosis and gonadal restructuring.</p>
},
  year = {2011},
  journal = {Comp Biochem Physiol B Biochem Mol Biol},
  volume = {158},
  pages = {56-63},
  month = {2011 Jan},
  issn = {1879-1107},
  doi = {10.1016/j.cbpb.2010.09.009},
  language = {eng},
}