Domain organization and phylogenetic analysis of proteins from the chitin deacetylase gene family of Tribolium castaneum and three other species of insects
| Autor: | Radhika Dixit, Richard W. Beeman, Charles A. Specht, Karl J. Kramer, Yasuyuki Arakane, Subbaratnam Muthukrishnan, Chad Richard |
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| Rok vydání: | 2007 |
| Předmět: |
0106 biological sciences
Signal peptide Molecular Sequence Data Groups Chitin Sequence alignment 01 natural sciences Biochemistry Amidohydrolases 03 medical and health sciences chemistry.chemical_compound Catalytic Domain Anopheles Gene family Animals Amino Acid Sequence Peptide sequence Molecular Biology Phylogeny 030304 developmental biology Genetics 0303 health sciences Tribolium Phylogenetic analysis biology fungi Intron Chromosome Mapping Exons Sequence Analysis DNA Bees biology.organism_classification Introns 3. Good health Chitin deacetylase Insects 010602 entomology Apis chemistry Structural Homology Protein Insect Science Multigene Family Drosophila Drosophila melanogaster Sequence Alignment |
| Zdroj: | Insect biochemistry and molecular biology. 38(4) |
| ISSN: | 0965-1748 |
| Popis: | A bioinformatics investigation of four insect species with annotated genome sequences identified a family of genes encoding chitin deacetylase (CDA)-like proteins, with five to nine members depending on the species. CDAs (EC 3.5.1.41) are chitin-modifying enzymes that deacetylate the β-1,4-linked N-acetylglucosamine homopolymer. Partial deacetylation forms a heteropolysaccharide that also contains some glucosamine residues, while complete deacetylation produces the homopolymer chitosan, consisting exclusively of glucosamine. The genomes of the red flour beetle, Tribolium castaneum, the fruit fly, Drosophila melanogaster, the malaria mosquito, Anopheles gambiae, and the honey bee, Apis mellifera contain 9, 6, 5 and 5 genes, respectively, that encode proteins with a chitin deacetylase motif. The presence of alternative exons in two of the genes, TcCDA2 and TcCDA5, increases the protein diversity further. Insect CDA-like proteins were classified into five orthologous groups based on phylogenetic analysis and the presence of additional motifs. Group I enzymes include CDA1 and isoforms of CDA2, each containing in addition to a polysaccharide deacetylase-like catalytic domain, a chitin-binding peritrophin-A domain (ChBD) and a low-density lipoprotein receptor class A domain (LDLa). Group II is composed of CDA3 orthologs from each insect species with the same domain organization as group I CDAs, but differing substantially in sequence. Group III includes CDA4s, which have the ChBD domain but do not have the LDLa domain. Group IV comprises CDA5s, which are the largest CDAs because of a very long intervening region separating the ChBD and catalytic domains. Among the four insect species, Tribolium is unique in having four CDA genes in group V, whereas the other insect genomes have either one or none. Most of the CDA-like proteins have a putative signal peptide consistent with their role in modifying extracellular chitin in both cuticle and peritrophic membrane during morphogenesis and molting. |
| Databáze: | OpenAIRE |
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