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Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
Published on: March 24, 2012
Proteomics analysis of the endogenous, constitutive, leaf SUMOylome
Bertrand Colignon1, Edouard Delaive2, Marc Dieu3
1Département Sciences du Vivant, Centre wallon de Recherches agronomiques, chaussée de Charleroi 234, 5030 Gembloux, Belgium; URBC-NARILIS, Université de Namur, rue de Bruxelles 61, 5000 Namur, Belgium.
Abstract:
SUMOylation is a post-translational modification which regulates a number of critical biological processes in, for example mammals, yeast and plants. In order to fully understand the functional effects of SUMOylation an essential first step is the identification of endogenous targets for SUMOylation. Here we report the results of using a recently developed proteomic approach based on the use of 3D gels to identify the endogenous SUMO targets in leaves of Solanum tuberosum. By using 3D gels we avoid the problem of co-migration of proteins, which is a major limitation of 2D gels, and we enable the use of the highly sensitive CyDye DIGE fluor saturation dyes. Using this new method we have identified 39 individual proteins as probable SUMO targets in leaves of Solanum tuberosum. The advantages of this method compared with other approaches are discussed, and possible future developments are outlined.
Significance:
The authors have no conflicts of interest to declare. All authors have approved the manuscript and agree with submission to Journal of Proteomics.

