title: Identification of SUMO targets by a novel proteomic approach in plants(F).
abstract: Post-translational modifications (PTMs) chemically and physically alter the properties of proteins, including their folding, subcellular localization, stability, activity, and consequently their function. In spite of their relevance, studies on PTMs in plants are still limited. Small Ubiquitin-like Modifier (SUMO) modification regulates several biological processes by affecting protein-protein interactions, or changing the subcellular localizations of the target proteins. Here, we describe a novel proteomic approach to identify SUMO targets that combines 2-D liquid chromatography, immunodetection, and mass spectrometry (MS) analyses. We have applied this approach to identify nuclear SUMO targets in response to heat shock. Using a bacterial SUMOylation system, we validated that some of the targets identified here are, in fact, labeled with SUMO1. Interestingly, we found that GIGANTEA (GI), a photoperiodic-pathway protein, is modified with SUMO in response to heat shock both in vitro and in vivo.
authors.affiliation: Centro de Biotecnología y Genómica de Plantas INIA-UPM, Campus de Montegancedo, Madrid 28223, Spain.
authors.forename: Gema
authors.initials: G
authors.lastname: López-Torrejón
authors.forename: Davide
authors.initials: D
authors.lastname: Guerra
authors.forename: Rafael
authors.initials: R
authors.lastname: Catalá
authors.forename: Julio
authors.initials: J
authors.lastname: Salinas
authors.forename: Juan C
authors.initials: JC
authors.lastname: del Pozo
mesh_terms: D002853:Chromatography, Liquid; D006358:Hot Temperature; D013058:Mass Spectrometry; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D040901:Proteomics; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*; D013312:Stress, Physiological
chemical_list: D010940:Plant Proteins; D025841:Small Ubiquitin-Related Modifier Proteins