Abstract
A cDNA clone (pcM12) of the chalcone synthase (CHS) ofMatthiola incana R. Br. (Brassicacease) was isolated from a cDNA library, sequenced and analysed. It comprises the complete coding sequence for the CHS and 5′ and 3′ untranslated regions. The deduced amino acid sequence shows that theMatthiola incana CHS consists of 394 amino acid residues. Comparison with CHS amino acid sequences of other plants indicates more than 82% homology.
References
Ehmann B, Schäfer E: Nucleotide sequences encoding two different chalcone synthases expressed in cotyledons of SAN 9798 treated mustard (Sinapis alba L.). Plant Mol Biol 11: 869–870 (1988).
Elliston K, Messing J: The molecular architecture of plant genes. A phylogenetic perspective. In: Kahl G (ed) Architecture of Eukaryotic Genes VCH Verlagsgesellschaft, Weinheim (1988).
Feinbaum RL, Ausubel FM: Transcriptional regulation of theArabidopsis thaliana chalcone synthase gene. Mol Cell Biol 8: 1985–1992 (1988).
Herrmann A, Schulz W, Hahlbrock K: Two alleles of the single-copy chalcone synthase gene in parsley differ by a transposon-like element. Mol Gen Genet 212: 93–98 (1988).
Koes RE, Spelt CE, van den Elzen PJM, Mol JNM: Cloning and molecular characterization of the chalcone synthase multigene family ofPetunia hybrida. Gene 81: 245–257 (1989).
Kreuzaler F, Ragg H, Fautz E, Kuhn DN, Hahlbrock K: UV induction of chalcone synthase mRNA in cell suspension cultures ofPetroselinum hortense. Proc Natl Acad Sci USA 80: 2591–2593 (1983).
Maniatis T, Fritsch EF, Sambrook J: Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY (1982).
Myers EW, Miller W: Optimal alignments in linear space. In: CABIOS 4: 11–17 (1988).
Niesbach-Klösgen U, Barzen E, Bernhardt J, Rohde W, Schwarz-Sommer Z, Reif HJ, Wienand U, Saedler H: Chalcone synthase genes in plants: A tool to study evolutionary relationships. J Mol Evol 26: 213–225 (1987).
Dean C, Tamaki S, Dunsmuir P, Favreau M, Katayama C, Dooner H, Bedbrood J: mRNA transcripts of several plant genes are polyadenylated at multiple sites in vivo. Nucl Acids Res 14: 2229–2240 (1986).
Pustell J, Katafos FC: A convenient and adaptable package of computer programs for DNA and protein sequence management, analysis, and homology determination. Nucl Acids Res 12: 643–655 (1984).
Rall S, Hemleben V: Characterization and expression of chalcone synthase in different genotypes ofMatthiola incana R. Br. during flower development. Plant Mol Biol 3: 137–145 (1984).
Reif HJ, Niesback U, Deumling B, Saedler H: Cloning and analysis of two genes for chalcone synthase fromPetunia hydrida. Mol Gen Genet 199: 208–215 (1985).
Reimold U, Kröger M, Kreuzaler F, Hahlbrock K: Coding and 3′ non-coding nucleotide sequence of chalcone synthase mRNA and assignment of amino acid sequence of the enzyme. EMBO J 2: 1801–1805 (1983).
Ryder TB, Hedrick SA, Bell JN, Liang X, Clouse SD, Lamb CJ: Organization and differential activation of a gene family encoding the plant defence enzyme chalcone synthase inPhaseolus vulgaris. Mol Gen Genet 210: 219–233 (1987).
Sanger F, Nicklen S, Coulson AR: DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 74: 5463–5467 (1977).
Schwarz-Sommer Z, Gierl A, Cuypers H, Peterson PA, Saedler H: Plant transposable elements generate the DNA sequence diversity needed in evolution. EMBO J 4: 591–597 (1985).
Sommer H, Saedler H: Structure of the chalcone synthase gene ofAntirrhinum majus. Mol Gen Genet 202: 429–434 (1986).
Werner D, Chemla Y, Herzberg M: Isolation of poly(A)+ RNA by paper affinity chromatography. Anal Biochem 141: 329–336 (1984).
Wienand U, Weydemann U, Niesbach-Klösgen U, Peterson PA, Saedler H: Molecular cloning of the c2 locus ofZea mays, the gene coding for chalcone synthase. Mol Gen Genet 203: 202–207 (1986).
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Epping, B., Kittel, M., Ruhnau, B. et al. Isolation and sequence analysis of a chalcone synthase cDNA ofMatthiola incana R. Br. (Brassicaceae). Plant Mol Biol 14, 1061–1063 (1990). https://doi.org/10.1007/BF00019405
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DOI: https://doi.org/10.1007/BF00019405