Abstract
Eighty-six plant chitinase sequences from 29 different species and one hybrid were obtained from the on-line GenBank nucleotide database. These sequences were grouped into five gene families based on previously published guidelines (Meins et al., 1994), and the amino-acid and nucleotide sequences of each gene family were aligned. Consensus amino-acid and nucleotide sequences were derived for each gene family based on the alignments. The consensus sequences were analyzed to determine, their amino-acid composition, hydropathy profiles, and codon usage.
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Altschul, S.F., W. Gish, W. Miller, E.W. Myers, D.J. Lipman. 1990. Basic local alignment search tool. J. Mol. Biol. 215:403–410.
Broglie, K., I. Chet, M. Holliday, R. Cressman, P. Biddle, S. Knowlton, C. Mauvais, R. Broglie. 1991. Transgenic plants with enhanced resistance to the fungal pathogenRhizoctonia solani. Science. 254:1194–1197.
Kyte, J. and R. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105–132.
Lawton, K. A., J. Beck, S. Potter, E. Ward, J. Ryals. 1994. Regulation of cucumber Class III chitinase gene expression. Mol. Plant-Microbe Interact. 7 (1):48–57.
Meins, F., and P. Ahl. 1989. Induction of chitinase and b-1, 3-glucanase in tobacco plants infected withPseudomonas tabaci andPhytophthora parasitica var. nicotianae. Plant Sci. 61:155–161.
Meins, F., B. Fritig, H. J. M. Linthorst, J. Mikkelsen, J.-M. Neuhaus, J. Ryals. 1994. Plant chitinase genes. Plant Mol. Biol. Reptr. 12(2):S22-S28.
Neuhaus, J.-M., B. Fritig, H.J.M. Linthorst, F. Meins, J.D. Mikkelsen, J. Ryals. 1996. A revised nomenclature for chitinase genes. Plant Mol. Biol. Reptr. 14(2):102–104.
Schlumbaum, A., F. Mauch, U. Vogeli, T. Boller. 1986. Plant chitinases are potent inhibitors of fungal growth. Nature. 324:365–367.
Shinshi, H., J.-M. Neuhaus, J. Ryals, F. Meins. 1990. Structure of a tobacco endochitinase gene: Evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain. Plant Mol. Biol. 14:357–368.
Tsujibo, H., H. Orikoshi, C. Imada, Y. Okami, K. Miyamoto, Y. Inamori. 1993. Site-directed mutagenesis of chitinase fromAlteromonas sp. strain O-7. Biosci. Biotech. Biochem. 57(8):1396–1397.
Van Scheltinga, A.C.T., S. Armand, K.H. Kalk, A. Isogai B. Henrissat, B. W. Dijkstra. 1995. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis. Biochemistry. 34:15619–15623.
Verburg, J., S. Rangwala, D. Samac, V. Luckow, Q. Huynh. 1993. Examination of the role of tyrosine-174 in the catalytic mechanism of theArabidopsis thaliana chitinase: Comparison of variant chitinases generated by site-directed mutagenesis and expressed in insect cells using baculovirus vectors. Arch. Biochem. Biophys. 300(1):223–230.
Watanabe, T., K. Kobori, M. Kiyotaka, T. Fujii, H. Sakai, M. Uchida, H. Tanaka. 1993. Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 ofBacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem. 268(25):18567–18572.
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Levorson, J., Chlan, C.A. Plant chitinase consensus sequences. Plant Mol Biol Rep 15, 122–133 (1997). https://doi.org/10.1007/BF02812262
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DOI: https://doi.org/10.1007/BF02812262