J Integr Plant Biol. ›› 2009, Vol. 51 ›› Issue (2): 207-223.DOI: 10.1111/j.1744-7909.2008.00787.x

• Molecular Physiology • Previous Articles    

Analysis of the Arabidopsis Floral Proteome: Detection of over 2 000 Proteins and Evidence for Posttranslational Modifications

Baomin Feng, Lianchao Li, Xiaofan Zhou, Bruce Stanley and Hong Ma   

  • Received:2008-06-09 Accepted:2008-06-11 Published:2009-02-10


The proteome of the Arabidopsis flower has not been extensively studied previously. Here, we report a proteomic analysis of the wild type Arabidopsis flower. Using both two-dimensional electrophoresis/mass spectrometry (2-DGE/MS) and multi-dimensional protein identification technology (MudPIT) approaches, we identified 2 446 proteins. Although a single experiment or analysis uncovered only a subset of the proteins we identified, a combination of multiple experiments and analyses facilitated the detection of a greater number of proteins. When proteins are grouped according to RNA expression levels revealed by microarray experiments, we found that proteins encoded by genes with relatively high levels of expression were detected with greater frequencies. On the other hand, at the level of the individual gene/protein, there was not a good correlation between protein spot intensity and microarray values. We also obtained strong evidence for post-translational modification from 2-DGE and MudPIT data. We detected proteins that are annotated to function in protein synthesis, folding, modification, and degradation, as well as the presence of regulatory proteins such as transcription factors and protein kinases. Finally, sequence and evolutionary analysis of genes for active methyl group metabolisms suggests that these genes are highly conserved. Our results allow the formulation of hypotheses regarding post-translational regulation of proteins in the flower, providing new understanding about Arabidopsis flower development and physiology.

Key words: Arabidopsis, floral, methylation, multi-dimensional protein identification technology, protein modification, proteome

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