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Citation
Shen, Z., Jacobs-Lorena, M. (1999). Evolution of chitin-binding proteins in invertebrates.  J. Mol. Evol. 48(3): 341--347.
FlyBase ID
FBrf0108362
Publication Type
Research paper
Abstract

Analysis of a group of invertebrate proteins, including chitinases and peritrophic matrix proteins, reveals the presence of chitin-binding domains that share significant amino acid sequence similarity. The data suggest that these domains evolved from a common ancestor which may be a protein containing a single chitin-binding domain. The duplication and transposition of this chitin-binding domain may have contributed to the functional diversification of chitin-binding proteins. Sequence comparisons indicated that invertebrate and plant chitin binding domains do not share significant amino acid sequence similarity, suggesting that they are not coancestral. However, both the invertebrate and the plant chitin-binding domains are cysteine-rich and have several highly conserved aromatic residues. In plants, cysteines have been elucidated in maintaining protein folding and aromatic amino acids in interacting with saccharides <up>Wright HT, Sanddrasegaram G, Wright CS (1991) J Mol Evol 33:283-294 </up>. It is likely that these residues perform similar functions in invertebrates. We propose that the invertebrate and the plant chitin-binding domains share similar mechanisms for folding and saccharide binding and that they evolved by convergent evolution. Furthermore, we propose that the disulfide bonds and aromatic residues are hallmarks for saccharide-binding proteins.

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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    J. Mol. Evol.
    Title
    Journal of Molecular Evolution
    Publication Year
    1971-
    ISBN/ISSN
    0022-2844
    Data From Reference
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    Genes (1)