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JXB Advance Access originally published online on January 22, 2007
Journal of Experimental Botany 2007 58(5):1151-1160; doi:10.1093/jxb/erl288
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© The Author [2007]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

RESEARCH PAPER

Isolation and characterization of a tomato non-specific lipid transfer protein involved in polygalacturonase-mediated pectin degradation

Monic M. M. Tomassen1,*, Diane M. Barrett2, Henry C. P. M. van der Valk1 and Ernst J. Woltering1

1Wageningen University and Research Center, Agrotechnology and Food Innovations, PO Box 17, 6700 AA Wageningen, The Netherlands
2Department of Food Science and Technology, University of California, Davis, CA 95616-8598, USA

* To whom correspondence should be addressed. E-mail: Monic.Tomassen{at}wur.nl

An important aspect of the ripening process of tomato fruit is softening. Softening is accompanied by hydrolysis of the pectin in the cell wall by pectinases, causing loss of cell adhesion in the middle lamella. One of the most significant pectin-degrading enzymes is polygalacturonase (PG). Previous reports have shown that PG in tomato may exist in different forms (PG1, PG2a, PG2b, and PGx) commonly referred to as PG isoenzymes. The gene product PG2 is differentially glycosylated and is thought to associate with other proteins to form PG1 and PGx. This association is thought to modulate its pectin-degrading activity in planta. An 8 kDa protein that is part of the tomato PG1 multiprotein complex has been isolated, purified, and functionally characterized. This protein, designated ‘activator’ (ACT), belongs to the class of non-specific lipid transfer proteins (nsLTPs). ACT is capable of ‘converting’ the gene product PG2 into a more active and heat-stable form, which increases PG-mediated pectin degradation in vitro and stimulates PG-mediated tissue breakdown in planta. This finding suggests a new, not previously identified, function for nsLTPs in the modification of hydrolytic enzyme activity. It is proposed that ACT plays a role in the modulation of PG activity during tomato fruit softening.

Key words: Activator, convertor, fruit ripening, fruit softening, lipid transfer protein, Lycopersicon esculentum, polygalacturonase, ß-subunit, tomato

Received 18 September 2006; Accepted 20 November 2006


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