Summary
A disulfide-rich domain, first identified in wheat germ agglutinin, has now been identified in the amino acid and DNA sequences of a large number of other chitin-binding proteins. This 43-residue domain includes eight disulfide-linked cysteines and has been implicated in the binding ofN-acetylglucosamine and its polymers. This study used 12 complementary DNA sequences and 1 amino acid sequence of proteins with one, two, and four copies of this domain to infer a 44-amino acid residue ancestor sequence for this domain, and to derive an evolutionary tree relating these domains in the different proteins. The tree relating these single-domain sequences is divided into two major branches, one consisting of the multidomain dimeric lectins, which we have earlier suggested arose by duplication of a single copy of the disulfide-rich domain, and the other branch consisting of the monomeric chitinases and wound-inducible proteins, which have a single copy of the domain fused to a larger polypeptide. Reference to the three-dimensional structure of WGA and its saccharide complexes shows that the saccharide-binding residues as well as cysteine and glycine residues are conserved among all available sequences. In contrast, many residues at the dimer interface of the domains of WGA are not conserved in those proteins with a single domain, implying that the aggregation state of the domains in these proteins differs from that of the grass lectins. Also, the base compositions of the four-domain and one-domain branches of the tree differ, indicating distinct selective pressures at the level of both protein structure and the gene or its transcript.
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Allen AK, Neuberger A, Sharon N (1973) The purification, composition and specificity of wheat germ agglutinin. Biochem J 131:155–162
Blanken RL, Klotz LC, Hinnebusch AG (1982) Computer comparison of new and existing criteria for constructing evolutionary trees from sequence data. J Mol Evol 19:9–19
Blodgett JK, Loudon GM, Collins KD (1985) Specific cleavage of peptides containing an aspartic acid (β hydroxamic acid) residue. J Am Chem Soc 107:4305–4313
Broekaert WF, Van Parij J, Leyns F, Joos H, Peumans WJ (1989) A chitin binding lectin from stinging nettle rhizomes with antifungal properties. Science 245:1100–1102
Broekaert WF, Lee H, Kush A, Chua NH, Raikhel N (1990) Wound-induced accumulation of mRNA containing a hevein sequence in lactifers of rubber tree (Hevea brasiliensis). Proc Natl Acad Sci USA 87:7633–7637
Broglie KE, Gaynor JJ, Broglie RM (1986) Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase fromPhaseolus vulgaris. Proc Natl Acad Sci USA 83:6820–6824
Chapot MP, Peumans WJ, Strosberg AD (1986) Extensive homologies between lectins from non-leguminous plants. FEBS Lett 195:231–234
Chrispeels MJ, Raikhel NV (1990) Lectins, lectin genes and their role in plant defense. Plant Cell 3:1–9
Devereux J, Haeberli P, Smithies O (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12:387–395
Fitch W (1971) Toward defining the course of evolution: minimum change for a specific tree topology. Syst Zool 20:406–416
Geiger T, Clarke S (1987) Deamidation, isomerization, and recemization of asparaginyl and aspartyl residues in peptides: succinimide-linked reactions that contribute to protein degradation. J Biol Chem 262:785–794
Hilu KW, Wright K (1982) Systematics of gramineae: a cluster analysis study. Taxon 31:9–36
Jaeger JA, Turner DH, Zuker M (1989) Improved predictions of secondary structures for RNA. Proc Natl Acad Sci 86:7706–7710
Jaeger JA, Turner DH, Zuker M (1990) Predicting optimal and suboptinal secondary structures for RNA. In: Doolittle RF (ed) Molecular evolution: computer analysis of protein and nucleic acid sequences. Methods in enzymology, vol 183. Academic Press, New York, pp 281–306
Jones TA (1978) A graphics model building and refinement system for macromolecules. J Appl Cryst 11:268–272
Klotz LC, Blanken RL (1981) A practical method for calculating evolutionary trees from sequence data. J Theor Biol 91:261–272
Klotz LC, Komar N, Blanken RL, Mitchell RM (1979) Calculation of evolutionary trees from sequence data. Proc Natl Acad Sci USA 76:4516–4520
Lerner DR, Raikhel NV (1989) Cloning and characterization of root specific barley lectin. Plant Physiol 91:124–129
Lucas J, Henschen A, Lottspeich F, Voegeli U, Boller T (1985) Amino-terminal sequence of ethylene-induced bean leaf chitinase reveals similarities to sugar-binding domains of wheat germ agglutinin. FEBS Lett 193:208–210
Matassi G, Montero LM, Salinas J, Bernardi G (1989) The isochore organization and the compositional distribution of homologous coding sequences in the nuclear genome of plants. Nucleic Acids Res 17:5273–5290
Murdock LL, Heusing JE, Nielsen SS, Pratt RC, Shade RE (1990) Biological effects of plant lectins on the cowpea weevil. Phytochemistry 29:85–89.
Parsons TJ, Bradshaw HD, Gordon MP (1989) Systemic accumulation of specific mRNAs in response to wounding of poplar trees. Proc Natl Acad Sci USA 86:7895–7899
Peumans WJ, DeLey M, Broekaert WF (1984) An unusual lectin from stinging nettle (Urtica dioica) rhizomes. FEBS Lett 177:99–102
Raikhel NV, Wilkins TA (1987) Isolation and characterization of a cDNA clone encoding wheat germ agglutinin. Proc Natl Acad Sci USA 84:6745–6749
Rice RH (1976) Wheat germ agglutinin: evidence for a genetic basis of multiple forms. Biochim Biophys Acta 444:175–180
Rice RH, Etzler ME (1975) Chemical modification and hybridization of wheat germ agglutinins. Biochemistry 14:4093–4099
Schlumbaum A, Mauch F, Vogeli U, Boller T (1986) Plant chitinases are potent inhibitors of fungal growth. Nature (London) 324:365–367
Shinshi H, Mohnen D, Meins F Jr (1987) Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissue by auxin and cytokinin. Proc Natl Acad Sci USA 84:89–93
Shinshi H, Neuhaus J-M, Ryals J, Meins F (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
Smith JJ, Raikhel NV (1989) Nucleotide sequence of cDNA clones encoding wheat germ agglutinin isolectins A and D. Plant Mol Biol 13:601–603
Stanford A, Bevan M, Northcote D (1989) Differential expression within a family of novel wound-induced genes in potato. Mol Gen Genet 215:200–208
Van Parij J, Broekaert WF, Goldstein IJ, Peumans WJ (1991) Hevein: an antifungal protein from rubber tree (Hevea brasiliensis) latex. Planta 183:258–264
Voorter CEM, de Haard-Hoekman WA, van den Oetelaar PJM, Bloemendal H, de Jong WW (1988) Spontaneous peptide bond cleavage in aging α-crystallin through a succinimide intermediate. J Biol Chem 263:19020–19023
Walujono K, Scholma RA, Beintema JJ, Marjiono A, Hahn AM (1975) Amino acid sequence of hevein. In: Proceedings of the International Rubber Conference, Kuala Lumpur, pp 518–531, also in Dayhoff MO (ed) Atlas of protein sequences and structure, vol 5, Suppl 3. National Biomedical Press, Washington DC, p 308
Wilkins TA, Raikhel NV (1989) Expression of rice lectin is governed by two temporally and spatially regulated mRNAs in developing embryos. Plant Cell 1:541–549
Wright CS (1977) The crystal structure of wheat germ agglutinin at 2.2Å resolution. J Mol Biol 111:439–457
Wright CS (1984) Structural comparison of the two distinct sugar binding sites in wheat germ agglutinin isolectin 2. J Mol Biol 178:91–104
Wright CS (1987) Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8Å resolution. J Mol Biol 194:501–529
Wright CS (1989) Comparison of the refined crystal structures of two wheat germ isolectins. J Mol Biol 209:475–487
Wright CS (1990) 2.2Å resolution structure analysis of two refinedN-acetylneuraminyl-lactose-wheat germ agglutinin isolectin complexes. J Mol Biol 215:635–651
Wright CS, Kahane I (1987) Preliminary x-ray diffraction results on co-crystals of wheat germ agglutinin with a sialoglycopeptide from the red cell receptor glycophorin A. J Mol Biol 194:353–355
Wright CS, Raikhel N (1989) Sequence variability of three wheat germ agglutinin isolectins: products of multiple genes in polyploid wheat. J Mol Evol 28:327–336
Wright HT, Brooks DM, Wright CS (1985) Evolution of the multidomain protein wheat germ agglutinin. J Mol Evol 21:133–138
Zuker M (1989) On finding all suboptimal foldings of an RNA molecule. Science 244:48–52
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Wright, H.T., Sandrasegaram, G. & Wright, C.S. Evolution of a family ofN-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin. J Mol Evol 33, 283–294 (1991). https://doi.org/10.1007/BF02100680
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DOI: https://doi.org/10.1007/BF02100680