J. Biol. Chem., Vol. 265, Issue 29, 17451-17455, 10, 1990
Molecular cloning of wheat dihydrodipicolinate synthase
T Kaneko, T Hashimoto, R Kumpaisal and Y Yamada
Research Center for Cell and Tissue Culture, Faculty of Agriculture, Kyoto University, Japan.
Four forms of dihydrodipicolinate synthase (DHDPS), which catalyzes the
first reaction in the lysine-specific biosynthetic pathway in higher
plants, were purified to homogeneity from a suspension culture of wheat
(Triticum aestivum). These polypeptides have similar N-terminal amino acid
sequences. Two different cDNA clones were isolated by screening a wheat
cDNA library with oligonucleotide probes based on these amino acid
sequences. The predicted amino acid sequences indicate that both clones
encode putative chloroplast transit peptides that have little homology to
each other as well as the conserved mature protein portions of Mr 35,737
and 35,776 (94% identity). Mature wheat DHDPS has 30% amino acid identity
to Escherichia coli DHDPS. One of the cloned cDNAs, which had been fused to
bacterial transcription/translation signals, genetically complemented a
strain of E. coli that lacks endogenous DHDPS activity. Moreover, the
expression of wheat DHDPS cDNA in wild- type E. coli increased the
enzymatic activity 10-fold in the transformed bacteria.
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