Abstract
A poplar DHDPS cDNA clone has been isolated by functional rescue of thedapA-deficient AT997 mutant ofEscherichia coli. By sequence comparison between the poplar and maize DHDPS cDNAs, two oligonucleotides were designed to perform polymerase chain reaction (PCR) onArabidopsis thaliana genomic DNA. The PCR fragment was subsequently used to isolate anArabidopsis DHDPS genomic and cDNA clone.
References
Negrutiu J, Cattoir-Reynearts A, Verbruggen I, Jacobs M: Lysine overproducer mutants with an altered dihydrodipicolinate synthase from protoplast culture ofNicotiana sylvestris. Theor Applied Genet 68: 11–20 (1984).
Vernaillen S, Van Ghelue M, Verbruggen I, Jacobs M: Characterization of mutants inArabidopsis thaliana resistant to analogues and inhibitory concentrations of amino acids derived from aspartate. Arabidopsis Inf Serv 22: 13–20 (1985).
Frankard V, Ghislain M, Jacobs M: Two feedback-insensitive enzymes of the aspartate pathway inNicotiana sylvestris. Plant Physiol 99: 1285–1293 (1992).
Kumpaisal R, Hashimoto T, Yamada Y: Purification and characterization of dihydrodipicolinate synthase from wheat suspension cultures. Plant Physiol 85: 145–151 (1987).
Frisch D, Gengenbach B, Tommey A, Sellner J, Somers D, Myers D: Isolation and characterization of dihydrodipicolinate synthese from maize. Plant Physiol 96: 444–452 (1991).
Ghislain M, Frankard V, Jacobs M: Dihydrodipicolinate synthase ofNicotiana sylvestris, a chloroplast-localized enzyme of the lysine pathway. Planta 180: 480–486 (1990).
Laber B, Gomis-Rüth F, Romao M, Huber R:Escherichia coli dihydrodipicolinate synthase: identification of the active site and crystallization. Biochem J 288: 691–695 (1992).
Perl A, Shaul O, Galili G: Regulation of lysine synthesis in transgenic potato plants expressing a bacterial dihydrodipicolinate synthase in their chloroplasts. Plant Mol Biol 19: 815–823 (1992).
Shaul O, Galili G: Increased lysine synthesis in tobacco plants that express high levels of bacterial dihydrodipicolinate synthase in their chloroplasts. Plant J: 203–209 (1992).
Taneko T, Hashimoto T, Kumpaisal R, Yamada Y: Molecular cloning of wheat dihydrodipicolinate synthase. J Biol Chem 265: 17451–17455 (1990).
Frish D, Tommey A, Gengenbach B, Somers D: Direct genetic selection of a maize cDNA for dihydrodipicolinate synthase in anEscerichia coli dapA auxotroph. Mol Gen Gent 228: 287–293 (1991).
Richaud F, Richaud C, Ratet P, Patte JC: Chromosomal location and nucleotide sequence of theEscherichia coli dapA gene. J Bact 166: 297–300 (1986).
Bonnassie S, Oreglia J, Sicard A: Nucleotide sequence of thedapA gene fromCorynebacterium glutamicum. Nucl Acids Res 18: 6421 (1990).
Nai-Young Chen, Shu-Qin Jiang, Klein D, Paulus H: Organization and nucleotide sequence of theBacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase. J Biol Chem 268: 9448–9465 (1993).
Dumas B, Van Doorsselaere J, Gielen J, Legrand M, Fritig B, Van Montagu M, Inzé D: Nucleotide sequence of a complementary DNA encodingO-methyltransferase from poplar. Plant Physiol 98: 796–797 (1992).
Feinberg A, Vogelstein B: A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 132: 6–13 (1983).
Lütcke H, Chow K, Mickel F, Moss K, Kern H, Schele G: Selection of AUG initiation codons differs in plants and animals. EMBO J 6: 43–48 (1987).
Gavel Y, von Heije G: A conserved cleavage-site motif in chloroplast transit peptides. FEBS Lett 261: 455–458 (1990).
von Heijne G, Steppuhn J, Herrmann R: Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180: 535–545 (1989).
Shedlarsky J, Gilvarg C: The pyruvate-aspartic semialdehyde condensing enzyme ofEscherichia coli. J Biol Chem 245: 1362–1373 (1970).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Vauterin, M., Jacobs, M. Isolation of a poplar and anArabidopsis thaliana dihydrodipicolinate synthase cDNA clone. Plant Mol Biol 25, 545–550 (1994). https://doi.org/10.1007/BF00043882
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00043882