期刊
PROTEOMICS
卷 11, 期 9, 页码 1720-1733出版社
WILEY
DOI: 10.1002/pmic.201000620
关键词
Arabidopsis; Mass spectra; Mitochondrial proteome; Multidimensional gel experiments; Plant proteomics; Phosphorylation
资金
- Australian Research Council (ARC)
- ARC Centre of Excellence in Plant Energy Biology
- United States Department of Energy, Office of Science, Office of Biological and Environmental Research, through the Joint BioEnergy Institute [DE-AC02-05CH11231]
Mitochondria undertake the process of oxidative phosphorylation yielding ATP for plant cell maintenance and growth. The principles of isolation and fractionation of plant mitochondrial proteins have been improved over decades, and surveys of the mitochondrial proteome in a number of plants species have been performed. Over time, many quantitative analyses of changes in the plant mitochondrial proteome have been performed by 2-D gel analyses revealing the induction, degradation and modification of mitochondrial proteins in responses to mutation, stress and development. Here, we present a saturating MS analysis of 2-D gel separable protein spots from a typical purification of Arabidopsis mitochondria identifying 264 proteins, alongside an LC-MS/MS survey by non-gel methods identifying 220 proteins. This allowed us to characterise the major mitochondrial proteins that are not observed on 2-D gels, the common contaminants and the abundance of the protein machinery of key mitochondrial biochemical pathways, and consider the impact of N-terminal pre-sequence cleavage and phosphorylation as explanations of multiple protein spots and the co-ordinates of proteins on 2-D gels.
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