Plant Physiol. Drug Metab Dispos
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Molecular Cloning and Tissue-Specific Expression of an Anionic Peroxidase in Zucchini1

Sabine Carpin, Michèle Crèvecoeur, Hubert Greppin, and Claude Penel*

Laboratoire de Biochimie et Physiologie Végétales, Université de Genève, Place de l'Université 3, CH-1211 Geneva, Switzerland

A calcium-pectate-binding anionic isoperoxidase (APRX) from zucchini (Cucurbita pepo) was purified and subjected to N-terminal amino acid microsequencing. The cDNA encoding this enzyme was obtained by reverse transcriptase polymerase chain reaction from a cDNA library. It encoded a mature protein of 309 amino acids exhibiting all of the sequence characteristics of a plant peroxidase. Despite the presence of a C-terminal propeptide, APRX was found in the apoplast. APRX protein and mRNA were found in the root, hypocotyls, and cotyledons. In situ hybridization showed that the APRX-encoding gene was expressed in many different tissues. The strongest expression was observed in root epidermis and in some cells of the stele, in differentiating tracheary elements of hypocotyl, in the lower and upper epidermis, in the palisade parenchyma of cotyledons, and in lateral and adventitious root primordia. In the hypocotyl hook there was an asymmetric expression, with the inner part containing more transcripts than the outer part. Treatment with 2,3,5-triiodobenzoic acid reduced the expression of the APRX-encoding gene in the lower part of the hypocotyl. Our observations suggest that APRX could be involved in lignin formation and that the transcription of its gene was related to auxin level.

1   This work was partly supported by the Federal Office of Education and Science (grant no. 93-0090). S.C. received a grant from the Agence Universitaire de la Francophonie.
*   Corresponding author: e-mail Claude.Penel{at}bota.unige.ch; fax 41-22-329-7795.

Plant Physiol. (1999) 120: 799-810
Copyright Clearance Center:   0032-0889/99/120//12
© 1999 American Society of Plant Physiologists




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