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Published on June 7, 2007; 10.1104/pp.107.096347


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Received January 24, 2007
Accepted May 19, 2007

Silencing of the Major Salt-dependent Isoform of Pectinesterase in Tomato Alters Fruit Softening

Thanh D. Phan , Wen. Bo , Gill. West , Grantley W. Lycett , and Gregory A. Tucker *

University of Nottingham, School of Biosciences, Sutton Bonington Campus, Loughborough, Leics. LE12 5RD, United Kingdom

* Corresponding author; email: gregory.tucker{at}nottingham.ac.uk.

Pectinesterase (E.C 3.1.1.11) (PE) is an enzyme responsible for the de-methylation 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 characterised by anti-sense 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.




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[Abstract] [Full Text] [PDF]




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