Proteome changes in tomato fruits prior to visible symptoms of chilling injury are linked to defensive mechanisms, uncoupling of photosynthetic processes and protein degradation machinery

A comparative proteomic analysis between tomato fruits stored at chilling and non-chilling temperatures was carried out just before the appearance of visible symptoms of chilling injury. At this stage of the stress period it was possible to discriminate between proteins involved in symptoms and proteins implicated in response. To investigate the changes in the tomato fruit proteome under this specific stressful condition, two-dimensional differential in-gel electrophoresis coupled with spot identification by mass spectrometry was applied. This proteomic approach allowed the identification of differentially expressed proteins which are involved in two main biological functions: (i) defensive mechanisms represented by small heat shock and late embryogenesis proteins; and (ii) reaction to the uncoupling of photosynthetic processes and the protein degradation machinery. One of the first changes observed in chilled fruits is the down-regulation of ATP synthase, 26S proteasome subunit RPN11 and aspartic proteinase, whereas the first responses in order to deal with the stress are mainly multifunctional proteins involved not only in metabolism but also in stress regulation such as glyceraldehyde phosphate dehydrogenase, 2-oxoglutarate dehydrogenase and invertase. In addition, our data seem to indicate a possible candidate to be used as a protein marker for further studies on cold stress: aldose-1-epimerase, which seems to have an important role in low temperature tolerance.This work was supported by the Spanish Ministry of Science and Innovation (MICINN) [grants PIE2009-40I080 and Plant KBBE 2009 EUI2009-04074]; the Agency of Science and Technology of the Region of Murcia (Spain) (Fundación SENECA) [grant 04553/GERM/06]; the Spanish Council of Scientific Research (CSIC) [post-doctoral positions from the JAE-Doc program conceded to P.S.B. and I.E.].Peer Reviewe