TY  - JOUR
A1  - Simm, Stefan
A1  - Papasotiriou, Dimitrios
A1  - Ibrahim, Mohamed
A1  - Leisegang, Matthias
A1  - Müller, Bernd
A1  - Schorge, Tobias
A1  - Karas, Michael
A1  - Mirus, Oliver
A1  - Sommer, Maik Sascha
A1  - Schleiff, Enrico
T1  - Defining the core proteome of the chloroplast envelope membranes
T2  - Frontiers in plant science : FPLS
N2  - High-throughput protein localization studies require multiple strategies. Mass spectrometric analysis of defined cellular fractions is one of the complementary approaches to a diverse array of cell biological methods. In recent years, the protein content of different cellular (sub-)compartments was approached. Despite of all the efforts made, the analysis of membrane fractions remains difficult, in that the dissection of the proteomes of the envelope membranes of chloroplasts or mitochondria is often not reliable because sample purity is not always warranted. Moreover, proteomic studies are often restricted to single (model) species, and therefore limited in respect to differential individual evolution. In this study we analyzed the chloroplast envelope proteomes of different plant species, namely, the individual proteomes of inner and outer envelope (OE) membrane of Pisum sativum and the mixed envelope proteomes of Arabidopsis thaliana and Medicago sativa. The analysis of all three species yielded 341 identified proteins in total, 247 of them being unique. 39 proteins were genuine envelope proteins found in at least two species. Based on this and previous envelope studies we defined the core envelope proteome of chloroplasts. Comparing the general overlap of the available six independent studies (including ours) revealed only a number of 27 envelope proteins. Depending on the stringency of applied selection criteria we found 231 envelope proteins, while less stringent criteria increases this number to 649 putative envelope proteins. Based on the latter we provide a map of the outer and inner envelope core proteome, which includes many yet uncharacterized proteins predicted to be involved in transport, signaling, and response. Furthermore, a foundation for the functional characterization of yet unidentified functions of the inner and OE for further analyses is provided.
KW  - membrane proteome
KW  - plant proteomics
KW  - chloroplast membrane proteins
KW  - mass spectrometry
KW  - envelope membrane proteome approach comparison
Y1  - 2013
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/28854
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-288545
SN  - 1664-462X
N1  - Copyright: © 2013 Simm, Papasotiriou, Ibrahim, Leisegang, Müller, Schorge, Karas, Mirus, Sommer and Schleiff. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
VL  - 4
IS  - Article 11
PB  - Frontiers Media
CY  - Lausanne
ER  -