Defining the core proteome of the chloroplast envelope membranes

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
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.
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Metadaten
Author:Stefan Simm, Dimitrios Papasotiriou, Mohamed Ibrahim, Matthias Leisegang, Bernd Müller, Tobias Schorge, Michael Karas, Oliver Mirus, Maik Sascha Sommer, Enrico Schleiff
URN:urn:nbn:de:hebis:30:3-288545
DOI:http://dx.doi.org/10.3389/fpls.2013.00011
ISSN:1664-462X
Pubmed Id:http://www.ncbi.nlm.nih.gov/pubmed?term=23390424
Parent Title (English):Frontiers in plant science : FPLS
Publisher:Frontiers Media
Place of publication:Lausanne
Document Type:Article
Language:English
Date of Publication (online):2013/02/06
Date of first Publication:2013/02/06
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2013/02/12
Tag:chloroplast membrane proteins; envelope membrane proteome approach comparison; mass spectrometry; membrane proteome; plant proteomics
Volume:4
Issue:Article 11
Pagenumber:18
Note:
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.
HeBIS PPN:331469979
Institutes:Biochemie und Chemie
Biowissenschaften
Dewey Decimal Classification:570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Sondersammelgebiets-Volltexte
Licence (German):License LogoCreative Commons - Namensnennung 3.0

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