Most organellar proteins are coded by the nucleus, synthesized in the cytosol and targeted specifically to subcellular compartments. Targeting to the many compartments operates with a complex machinery that relies on targeting sequences, cytosolic proteins and specific organellar receptors. Many studies have been done in attempt to characterize the steps involved in the localization of proteins, from the initial stages followed by its synthesis to the factors regulating its targeting. Cytosolic proteins that interact with dual-targeted proteins, verified with protein-protein interaction networks, will be used in studies of their role in the localization of organellar proteins in A. thaliana. This study will be performed by confirmation of these interactions in planta, using BiFC, and in vitro, with GST-pulldown; analysis of a possible co-regulation of gene expression between cytosolic proteins and their interactors; and analysis of gene silencing to verify the consequence of the absence of these cytosolic proteins to the correct localization of interacting proteins. These data may lead to the identification of proteins that are involved in the regulation of subcellular targeting of organellar proteins, such as dual-targeted proteins.
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