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PLANT PHYSIOLOGY , Vol 111, Issue 1 269-273, Copyright © 1996 by American Society of Plant Biologists
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GENE REGULATION AND MOLECULAR GENETICS |
A Cherry Protein and Its Gene, Abundantly Expressed in Ripening Fruit, Have Been Identified as Thaumatin-Like
B. R. Fils-Lycaon, P. A. Wiersma, K. C. Eastwell and P. Sautiere
Institut National de la Recherche Agronomique, Agroparc, Domaine Saint Paul, BP 91, Station de Technologie des Produits Vegetaux, 84914 Avignon cedex 9, France (B.R.F.-L.)
A 29-kD polypeptide is the most abundant soluble protein in ripe cherry
fruit (Prunus avium L); accumulation begins at the onset of ripening as the
fruit turns from yellow to red. This protein was extracted from ripe
cherries and purified by size-exclusion and ion-exchange chromatography.
Antibodies to the purified protein were used to screen a cDNA library from
ripe cherries. Numerous recombinant plaques reacted positively with the
antibodies; the DNA sequence of representative clones encoded a polypeptide
of 245 amino acid residues. A signal peptide was indicated, and the
predicted mature protein corresponded to the purified protein in size (23.3
kD, by mass spectrometry) and isoelectric point (4.2). A search of known
protein sequences revealed a strong similarity between this polypeptide and
the thaumatin family of pathogenesis-related proteins. The cherry
thaumatin-like protein does not have a sweet taste, and no antifungal
activity was seen in preliminary assays. Expression of the protein appears
to be regulated at the gene level, with mRNA levels at their highest in the
ripe fruit.
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