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Proteomic Analysis of MG132-Treated Germinating Pollen Reveals Expression Signatures Associated with Proteasome Inhibition
Authors:Candida Vannini  Marcella Bracale  Rita Crinelli  Valerio Marconi  Paola Campomenosi  Milena Marsoni  Valeria Scoccianti
Institution:1. Dipartimento di Biotecnologie e Scienze della Vita, Università degli Studi dell''Insubria, Varese, Italy.; 2. Dipartimento di Scienze Biomolecolari, Università di Urbino “Carlo Bo”, Urbino, Italy.; 3. Dipartimento di Scienze della Terra, della Vita e dell''Ambiente, Sezione di Biologia Vegetale, Università di Urbino “Carlo Bo”, Urbino, Italy.; St. Georges University of London, United Kingdom,
Abstract:Chemical inhibition of the proteasome has been previously found to effectively impair pollen germination and tube growth in vitro. However, the mediators of these effects at the molecular level are unknown. By performing 2DE proteomic analysis, 24 differentially expressed protein spots, representing 14 unique candidate proteins, were identified in the pollen of kiwifruit (Actinidia deliciosa) germinated in the presence of the MG132 proteasome inhibitor. qPCR analysis revealed that 11 of these proteins are not up-regulated at the mRNA level, but are most likely stabilized by proteasome inhibition. These differentially expressed proteins are predicted to function in various pathways including energy and lipid metabolism, cell wall synthesis, protein synthesis/degradation and stress responses. In line with this evidence, the MG132-induced changes in the proteome were accompanied by an increase in ATP and ROS content and by an alteration in fatty acid composition.
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