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PLANT PHYSIOLOGY , Vol 107, Issue 4 1083-1089, Copyright © 1995 by American Society of Plant Biologists
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GENE REGULATION AND MOLECULAR GENETICS |
Cloning and Characterization of Polyphenol Oxidase cDNAs of Phytolacca americana
R. W. Joy IV, M. Sugiyama, H. Fukuda and A. Komamine
Biological Institute, Faculty of Science, Tohoku University, Aoba-yama, Aoba-ku, Sendai 980, Japan
Two cDNA clones encoding polyphenol oxidases were isolated from a cDNA
library constructed from a log-phase suspension culture of Phytolacca
americana (pokeweed) producing betalains. The clones exhibit 93 and 86%
sequence identity at the nucleotide and deduced amino acid levels,
respectively. Both clones contain two copper-binding domains characterized
by histidine-rich regions, which are found ubiquitously in all polyphenol
oxidases/tyrosinases, and a putative third histidine-rich, copper-binding
region, which is common to all plant polyphenol oxidases. One of the
Phytolacca cDNA deduced amino acid sequences contains the ubiquitous
transit peptide for all proteins targeted to the internal lumen of
thylakoid membranes of plastids and is considered to be 98 residues in
length based on a proposed sequence cleavage site motif. This would produce
a processed peptide of approximately 54 kD. In addition to common features
of transit peptides, it was found that an additional conserved region for
polyphenol oxidases was located between the hydroxy amino acid-rich region
and the thylakoid transfer domain. Spatial and temporal expression was
investigated by northern blot analysis of total RNA from various organs of
Phytolacca plants. Transcripts of the two clones were found to be 2.1 and
2.3 kb, respectively. Both transcripts were present only at substantial
levels in ripening, betalain-containing fruit.
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