PMID- 31932409 OWN - NLM STAT- MEDLINE VI - 182 IP - 3 TI - Identification of Chloroplast Envelope Proteins with Critical Importance for Cold Acclimation. PG - 1239-1255 CI - © 2020 American Society of Plant Biologists. All Rights Reserved. LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - United States TA - Plant Physiol JT - Plant physiology JID - 0401224 IS - 1532-2548 (Electronic) LID - 10.1104/pp.19.00947 [doi] FAU - Trentmann, Oliver AU - Trentmann O AUID- ORCID: 0000-0002-9530-5848 AD - Technische Universität Kaiserslautern, Department of Biology, Plant Physiology, 67653 Kaiserslautern, Germany. FAU - Mühlhaus, Timo AU - Mühlhaus T AUID- ORCID: 0000-0003-3925-6778 AD - Technische Universität Kaiserslautern, Department of Biology, Computational Systems Biology, 67653 Kaiserslautern, Germany. FAU - Zimmer, David AU - Zimmer D AD - Technische Universität Kaiserslautern, Department of Biology, Computational Systems Biology, 67653 Kaiserslautern, Germany. FAU - Sommer, Frederik AU - Sommer F AD - Technische Universität Kaiserslautern, Department of Biology, Molecular Biotechnology and Systems Biology, 67653 Kaiserslautern, Germany. FAU - Schroda, Michael AU - Schroda M AUID- ORCID: 0000-0001-6872-0483 AD - Technische Universität Kaiserslautern, Department of Biology, Molecular Biotechnology and Systems Biology, 67653 Kaiserslautern, Germany. FAU - Haferkamp, Ilka AU - Haferkamp I AUID- ORCID: 0000-0002-7432-3190 AD - Technische Universität Kaiserslautern, Department of Biology, Plant Physiology, 67653 Kaiserslautern, Germany. FAU - Keller, Isabel AU - Keller I AUID- ORCID: 0000-0002-4989-1743 AD - Technische Universität Kaiserslautern, Department of Biology, Plant Physiology, 67653 Kaiserslautern, Germany. FAU - Pommerrenig, Benjamin AU - Pommerrenig B AUID- ORCID: 0000-0002-7522-7942 AD - Technische Universität Kaiserslautern, Department of Biology, Plant Physiology, 67653 Kaiserslautern, Germany. FAU - Neuhaus, Horst Ekkehard AU - Neuhaus HE AUID- ORCID: 0000-0002-5443-7123 AD - Technische Universität Kaiserslautern, Department of Biology, Plant Physiology, 67653 Kaiserslautern, Germany neuhaus@rhrk.uni-kl.de. IS - 0032-0889 (Linking) RN - 0 (Arabidopsis Proteins) RN - 0 (Chloroplast Proteins) RN - 0 (MEX1 protein, Arabidopsis) RN - 0 (Membrane Transport Proteins) SB - IM MH - Arabidopsis/metabolism MH - Arabidopsis Proteins/*metabolism MH - Chloroplast Proteins/*metabolism MH - Chloroplasts/*metabolism MH - Cold Temperature MH - Mass Spectrometry MH - Membrane Transport Proteins/metabolism MH - Proteomics PMC - PMC7054872 DCOM- 20210125 LR - 20231113 DP - 202003 DEP - 20200113 AB - 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 analyzed 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 under both 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 nucleotide transporter2 (NTT2; substantially increased abundance) or the maltose exporter MEX1 (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.