Analysis of the chloroplast proteome in arc mutants and identification of novel protein components associated with FtsZ2

• Published in: Plant molecular biology Vol. 81; no. 3; pp. 235 - 244
• Main Authors: Gargano, Daniela, Maple-Grødem, Jodi, Reisinger, Veronika, Eichacker, Lutz Andreas, Møller, Simon Geir
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.02.2013; Springer Nature B.V
• Subjects: Amino Acid Sequence; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis - physiology; Arabidopsis Proteins - metabolism; Biochemistry; Biomedical and Life Sciences; Chloroplast Proteins - metabolism; Chloroplasts; Chloroplasts - metabolism; Chloroplasts - physiology; Chromatography, High Pressure Liquid; Gene Expression Regulation, Plant; Life Sciences; Molecular biology; Mutation; Nicotiana - cytology; Nicotiana - genetics; Nicotiana - metabolism; Peptide Elongation Factor Tu - metabolism; Plant biology; Plant Leaves - genetics; Plant Leaves - metabolism; Plant Leaves - physiology; Plant Pathology; Plant Sciences; Plants, Genetically Modified; Plastids; Proteome; Proteomics; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Seedlings - genetics; Seedlings - metabolism; Seedlings - physiology; Tandem Mass Spectrometry; Two-Dimensional Difference Gel Electrophoresis; Two-Hybrid System Techniques; BN-PAGE; FtsZ; 2D-DIGE; LC–MS/MS; Chloroplast division
• ISSN: 0167-4412; 1573-5028
• DOI: 10.1007/s11103-012-9994-y

Chloroplasts are descendants of cyanobacteria and divide by binary fission. The number of chloroplasts is regulated in a cell type-specific manner to ensure that specialized cell types can perform their functions optimally. Several protein components of the chloroplast division apparatus have been identified in the past several years, but how this process is regulated in response to developmental status, environmental signals and stress is still unknown. To begin to address this we undertook a proteomic analysis of three accumulation and replication of chloroplasts mutants that show a spectrum of plastid division perturbations. We show that defects in the chloroplast division process results in changes in the abundance of proteins when compared to wild type, but that the profile of the native stromal and membrane complexes remains unchanged. Furthermore, by combining BN-PAGE with protein interaction assays we show that AtFtsZ2-1 and AtFtsZ2-2 assemble together with rpl12A and EF-Tu into a novel chloroplast membrane complex.