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Regulation and Functional Expression of Cinnamate 4-Hydroxylase from Parsley

Edda Koopmann, Elke Logemann, and Klaus Hahlbrock*

Max-Planck-Institut für Züchtungsforschung, Abteilung Biochemie, Carl-von-Linné-Weg 10, D-50829 Köln, Germany

A previously isolated parsley (Petroselinum crispum) cDNA with high sequence similarity to cinnamate 4-hydroxylase (C4H) cDNAs from several plant sources was expressed in yeast (Saccharomyces cerevisiae) containing a plant NADPH:cytochrome P450 oxidoreductase and verified as encoding a functional C4H (CYP73A10). Low genomic complexity and the occurrence of a single type of cDNA suggest the existence of only one C4H gene in parsley. The encoded mRNA and protein, in contrast to those of a functionally related NADPH:cytochrome P450 oxidoreductase, were strictly coregulated with phenylalanine ammonia-lyase mRNA and protein, respectively, as demonstrated by coinduction under various conditions and colocalization in situ in cross-sections from several different parsley tissues. These results support the hypothesis that the genes encoding the core reactions of phenylpropanoid metabolism form a tight regulatory unit.

*   Corresponding author; e-mail hahlbroc{at}mpiz-koeln.mpg.de; fax 49-221-506-2313.

Plant Physiol. (1999) 119: 49-56
Copyright Clearance Center:   0032-0889/99/119//08
© 1999 American Society of Plant Physiologists




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