Plant Molecular Biology

, Volume 79, Issue 4–5, pp 429–442 | Cite as

A functional pectin methylesterase inhibitor protein (SolyPMEI) is expressed during tomato fruit ripening and interacts with PME-1

  • Ida Barbara Reca
  • Vincenzo Lionetti
  • Laura Camardella
  • Rossana D’Avino
  • Thierry Giardina
  • Felice Cervone
  • Daniela Bellincampi


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.


Pectin 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.

Supplementary material

11103_2012_9921_MOESM1_ESM.ppt (6.4 mb)
Suppl. Figure 1 Nucleotide and deduced amino acid sequences of the SolyPMEI gene. Signal peptide end is indicated with a slash and the stop codon is marked with an asterisk. Putative N-glycosylation sites are gray boxed and sequence identified by 3′RACE is in bold and underlined and Arg 151 residue is highlighted. (PPT 6524 kb)
11103_2012_9921_MOESM2_ESM.ppt (6.2 mb)
Suppl. Figure 2 Motif analysis of SolyPMEI 5′ flanking region (-1500 bp). Red indicated AGAAA motif, green indicated CAAT box, yellow indicated TATA box and gray indicated AWTTCAA motif (PPT 6314 kb)
11103_2012_9921_MOESM3_ESM.ppt (6.2 mb)
Suppl. Figure 3 Circular dichroism spectra of SolyPMEI (continuous line) and AdPMEI from kiwi (dotted line) (PPT 6376 kb)
11103_2012_9921_MOESM4_ESM.ppt (6.2 mb)
Suppl. Figure 4 Sequence of tryptic fragments obtained by LS MS/MS analysis. Matched peptides are in bold and underlined (PPT 6302 kb)
11103_2012_9921_MOESM5_ESM.ppt (6.3 mb)
Suppl. Figure 5 Structural superimposition between SolyPMEI and AdPMEI. a Superimposition of Cα of all aligned residues of the SolyPMEI model (red) and AdPMEI structure (blue) (PDB code, 1XG2:B) (147 atoms) gave a RMSD of 0.13Å, indicating that SolyPMEI amino acid sequence well fits into the AdPMEI structure. No SolyPMEI residues were found out of the allowed regions of the Ramachandran plot; b PME-1/SolyPMEI model. PME-1 (left) is shown in blue and SolyPMEI (right) is shown in red. Glycosylated Asn residues of SolyPMEI are indicated (green) (PPT 6445 kb)


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Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Ida Barbara Reca
    • 1
    • 4
  • Vincenzo Lionetti
    • 1
  • Laura Camardella
    • 2
  • Rossana D’Avino
    • 2
  • Thierry Giardina
    • 3
  • Felice Cervone
    • 1
  • Daniela Bellincampi
    • 1
  1. 1.Dipartimento di Biologia e Biotecnologie “Charles Darwin”“Sapienza” Università di RomaRomeItaly
  2. 2.Institute of Protein Biochemistry, CNRNaplesItaly
  3. 3.ISM2/BiosCiences UMR CNRS 7313, Faculté des SciencesAix-Marseille Université, service 342Marseille Cedex 20France
  4. 4.Great Lakes Bioenergy Research CenterMichigan State UniversityEast LansingUSA

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