Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


First published online January 11, 2008; 10.1104/pp.107.112979

Plant Physiology 146:1040-1052 (2008)
© 2008 American Society of Plant Biologists

OPEN ACCESS ARTICLE
This Article
Free via Open Access: OA
Right arrow OA Full Text
Right arrow Full Text (PDF)
Right arrowOA All Versions of this Article:
146/3/1040    most recent
pp.107.112979v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (5)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sánchez-Pérez, R.
Right arrow Articles by Møller, B. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sánchez-Pérez, R.
Right arrow Articles by Møller, B. L.
Agricola
Right arrow Articles by Sánchez-Pérez, R.
Right arrow Articles by Møller, B. L.
BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

Bitterness in Almonds1,[C],[OA]

Raquel Sánchez-Pérez, Kirsten Jørgensen, Carl Erik Olsen, Federico Dicenta and Birger Lindberg Møller*

Plant Biochemistry Laboratory, Department of Plant Biology, Center for Molecular Plant Physiology (R.S.-P, K.J., B.L.M.), and Chemistry Department (C.E.O.), Faculty of Life Sciences, University of Copenhagen, DK–1871 Frederiksberg C, Copenhagen, Denmark; and Departamento de Mejora Vegetal, Centro de Edafología y Biología Aplicada del Segura-Consejo Superior de Investigaciones Científicas, E–30100 Murcia, Spain (F.D.)

Bitterness in almond (Prunus dulcis) is determined by the content of the cyanogenic diglucoside amygdalin. The ability to synthesize and degrade prunasin and amygdalin in the almond kernel was studied throughout the growth season using four different genotypes for bitterness. Liquid chromatography-mass spectrometry analyses showed a specific developmentally dependent accumulation of prunasin in the tegument of the bitter genotype. The prunasin level decreased concomitant with the initiation of amygdalin accumulation in the cotyledons of the bitter genotype. By administration of radiolabeled phenylalanine, the tegument was identified as a specific site of synthesis of prunasin in all four genotypes. A major difference between sweet and bitter genotypes was observed upon staining of thin sections of teguments and cotyledons for β-glucosidase activity using Fast Blue BB salt. In the sweet genotype, the inner epidermis in the tegument facing the nucellus was rich in cytoplasmic and vacuolar localized β-glucosidase activity, whereas in the bitter cultivar, the β-glucosidase activity in this cell layer was low. These combined data show that in the bitter genotype, prunasin synthesized in the tegument is transported into the cotyledon via the transfer cells and converted into amygdalin in the developing almond seed, whereas in the sweet genotype, amygdalin formation is prevented because the prunasin is degraded upon passage of the β-glucosidase-rich cell layer in the inner epidermis of the tegument. The prunasin turnover may offer a buffer supply of ammonia, aspartic acid, and asparagine enabling the plants to balance the supply of nitrogen to the developing cotyledons.


1 This work was supported by the Danish National Research Foundation (to the Center for Molecular Plant Physiology) and the Spanish Ministry of Education and Science, including a postdoctoral fellowship (to R.S.-P.).

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Birger Lindberg Møller (blm{at}life.ku.dk).

[C] Some figures in this article are displayed in color online but in black and white in the print edition.

[OA] Open Access articles can be viewed online without a subscription.

www.plantphysiol.org/cgi/doi/10.1104/pp.107.112979

* Corresponding author; e-mail blm{at}life.ku.dk.

Received November 13, 2007; accepted December 29, 2007; published January 11, 2008.




This article has been cited by other articles:


Home page
Plant Physiol.Home page
A. V. Morant, N. Bjarnholt, M. E. Kragh, C. H. Kjaergaard, K. Jorgensen, S. M. Paquette, M. Piotrowski, A. Imberty, C. E. Olsen, B. L. Moller, et al.
The {beta}-Glucosidases Responsible for Bioactivation of Hydroxynitrile Glucosides in Lotus japonicus
Plant Physiology, July 1, 2008; 147(3): 1072 - 1091.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2008 by the American Society of Plant Biologists