J Integr Plant Biol. ›› 2013, Vol. 55 ›› Issue (1): 96-107.DOI: 10.1111/jipb.12012

• Research Articles • Previous Articles     Next Articles

Identification of SUMO Targets by a Novel Proteomic Approach in Plants

Gema López-Torrejón1, Davide Guerra2, Rafael Catalá3, Julio Salinas3 and Juan C. del Pozo1*   

  1. 1Centro de Biotecnología y Genómica de Plantas (INIA-UPM), Campus de Montegancedo s/n. Autovía M-40, Km. 38. 28223 Pozuelo de Alarcón. Madrid, Spain
    2CRA-Genomics Research Centre (GPG), Via S. Protaso, 302. 29017, Fiorenzuela d'Arda (PC), Italy
    3Centro de Investigaciones Biológicas (CSIC), C/ Ramiro de Maeztu 9, Campus de la Ciudad Universitaria de Madrid, 28040 Madrid, Spain
  • Received:2012-08-16 Accepted:2012-11-04 Published:2013-01-01
  • About author:*Corresponding author. Tel: +34 91 336 4577; E-mail: jc.delpozo@upm.es

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.

Key words: SUMO, plants, post-translational modification, proteomics, mass spectrometry

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