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First published online June 7, 2007; 10.1104/pp.107.096347 Plant Physiology 144:1960-1967 (2007) © 2007 American Society of Plant Biologists
Silencing of the Major Salt-Dependent Isoform of Pectinesterase in Tomato Alters Fruit Softening1School of Biosciences, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire LE12 5RD, United Kingdom
Pectinesterase (PE; E.C. 3.1.1.11) is an enzyme responsible for the demethylation of galacturonyl residues in high-molecular-weight pectin and is believed to play an important role in cell wall metabolism. In this study, Pmeu1, a ubiquitously expressed PE gene, has been characterized by antisense suppression in tomato (Solanum lycopersicum). Transgenic tomato plants showed reduced PE activity levels in both green fruit and leaf tissue to around 65% and 25% of that found in wild-type plants, respectively. Pmeu1 was observed to encode a salt-dependent PE isoform that correlated with PE1 as previously described in fruit tissue. Silencing of Pmeu1 did not result in any detectable phenotype within the leaf tissue despite the gene product representing the major isoform in this tissue. In comparison, silencing in fruit resulted in an enhancement to the rate of softening during ripening. The role of PMEU1 in fruit ripening is discussed.
1 This work was supported by the Agri-Food Committee of the Biotechnology and Biological Sciences Research Council (studentship to T.D.P.) and by Overseas Research Studentship (to W.B.). 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: Gregory Tucker (gregory.tucker{at}nottingham.ac.uk). www.plantphysiol.org/cgi/doi/10.1104/pp.107.096347 * Corresponding author; e-mail gregory.tucker{at}nottingham.ac.uk; fax 44(0)1159–516122. Received January 24, 2007; accepted May 19, 2007; published June 7, 2007. This article has been cited by other articles:
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