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Plant Physiol. 2020 Jan 13. pii: pp.00947.2019. doi: 10.1104/pp.19.00947. [Epub ahead of print]

Identification of chloroplast envelope proteins with critical importance for cold acclimation.

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TU Kaiserslautern CITY: Kaiserslautern POSTAL_CODE: 67663 Germany [DE].
TU Kaiserslautern CITY: Kaiserslautern Germany [DE].
Technical University Kaiserslautern CITY: Kaiserslautern Germany [DE].
TU Kaiserslautern CITY: Kaiserslautern STATE: RLP POSTAL_CODE: 67663 Germany [DE].
TU Kaiserslautern CITY: Kaiserslautern POSTAL_CODE: D-67663 Germany [DE].
Technical University of Kaiserslautern CITY: Kaiserslautern STATE: Rh POSTAL_CODE: 0.67663 Germany [DE].
University of Kaiserslautern CITY: Kaiserslautern Germany [DE].
University of Kaiserslautern Pflanzenphysiologie, Postfach 3049 CITY: Kaiserslautern POSTAL_CODE: D-67653 Germany [DE]


The ability of plants to withstand cold temperatures relies on their photosynthetic activity. Thus, the chloroplast is of utmost importance for cold acclimation and acquisition of freezing tolerance. During cold acclimation, the properties of the chloroplast change markedly. To provide the most comprehensive view of the protein repertoire of the chloroplast envelope, we analysed this membrane system in Arabidopsis (Arabidopsis thaliana) using mass spectrometry-based proteomics. Profiling chloroplast envelope membranes was achieved by a cross comparison of protein intensities across the plastid and the enriched membrane fraction both under normal and cold conditions. We used multivariable logistic regression to model the probabilities for the classification of an envelope localization. In total, we identified 38 envelope membrane intrinsic or associated proteins exhibiting altered abundance after cold acclimation. These proteins comprise several solute carriers, such as the ATP/ADP antiporter NTT2 (nucleotide transporter 2, substantially increased abundance) or the maltose exporter MEX1 (maltose exporter 1, substantially decreased abundance). Remarkably, analysis of the frost recovery of ntt loss-of-function and mex1 overexpressor mutants confirmed that the comparative proteome is well suited to identify key factors involved in cold acclimation and acquisition of freezing tolerance. Moreover, for proteins with known physiological function, we propose scenarios explaining their possible roles in cold acclimation. Furthermore, spatial proteomics introduces an additional layer of complexity and enables the identification of proteins differentially localized at the envelope membrane under the changing environmental regime.

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