A functional pectin methylesterase inhibitor protein (SolyPMEI) is expressed during tomato fruit ripening and interacts with PME-1
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A pectin methylesterase inhibitor (SolyPMEI) from tomato has been identified and characterised by a functional genomics approach. SolyPMEI is a cell wall protein sharing high similarity with Actinidia deliciosa PMEI (AdPMEI), the best characterised inhibitor from kiwi. It typically affects the activity of plant pectin methylesterases (PMEs) and is inactive against a microbial PME. SolyPMEI transcripts were mainly expressed in flower, pollen and ripe fruit where the protein accumulated at breaker and turning stages of ripening. The expression of SolyPMEI correlated during ripening with that of PME-1, the major fruit specific PME isoform. The interaction of SolyPMEI with PME-1 was demonstrated in ripe fruit by gel filtration and by immunoaffinity chromatography. The analysis of the zonal distribution of PME activity and the co-localization of SolyPMEI with high esterified pectins suggest that SolyPMEI regulates the spatial patterning of distribution of esterified pectins in fruit.
KeywordsPectin methylesterification Pectin methylesterase inhibitor Fruit ripening Solanum lycopersicum
We would like to thank Prof. J. P. Knox for providing LM20 antibodies and Prof. M. E. Hendrickx for MA-TOM1-41B2 antibodies. This work was supported by the European Research Council (ERC Advanced Grant No. 233083), grant (C26A09RCP9) by “Sapienza” University of Rome, and by the Italian Ministry of Foreign Affairs.
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