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Molecular Cloning and Characterization of Apricot Fruit Polyphenol Oxidase

Tony Chevalier1, David de Rigal1, Didier Mbéguié-A-Mbéguié1, Frédéric Gauillard, Florence Richard-Forget*, and Bernard R. Fils-Lycaon

Institut National de la Recherche Agronomique, Site Agroparc, Domaine Saint Paul, Station de Technologie des Produits Végétaux, 84914 Avignon cedex 9, France (T.C., D.d.R., D.M.-A.-M., F.G., F.R.-F.); and Institut National de la Recherche Agronomique, Domaine Duclos, Station de Technologie des Produits Végétaux, B.P. 515, 97165 Pointe-à-Pitre cedex, French West Indies (B.R.F.-L.)

A reverse transcriptase-polymerase chain reaction experiment was done to synthesize a homologous polyphenol oxidase (PPO) probe from apricot (Prunus armeniaca var Bergeron) fruit. This probe was further used to isolate a full-length PPO cDNA, PA-PPO (accession no. AF020786), from an immature-green fruit cDNA library. PA-PPO is 2070 bp long and contains a single open reading frame encoding a PPO precursor peptide of 597 amino acids with a calculated molecular mass of 67.1 kD and an isoelectric point of 6.84. The mature protein has a predicted molecular mass of 56.2 kD and an isoelectric point of 5.84. PA-PPO belongs to a multigene family. The gene is highly expressed in young, immature-green fruit and is turned off early in the ripening process. The ratio of PPO protein to total proteins per fruit apparently remains stable regardless of the stage of development, whereas PPO specific activity peaks at the breaker stage. These results suggest that, in addition to a transcriptional control of PPO expression, other regulation factors such as translational and posttranslational controls also occur.


1   These authors contributed equally to this work.
*   Corresponding author; e-mail forget{at}avignon.inra.fr; fax 33-04-90-31-62-58.

Plant Physiol. (1999) 119: 1261-1270
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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