Plant Physiology Preview
Published on December 22, 2006; 10.1104/pp.106.090738
Received October 2, 2006
Accepted December 7, 2006
Proteome Dynamics during Plastid Differentiation in Rice (Oryza sativa L.)
Torsten Kleffmann , Anne von Zychlinski , Doris Russenberger , Matthias Hirsch-Hoffmann , Peter Gehrig , Wilhelm Gruissem , and Sacha Baginsky *
Institute of Plant Sciences, ETH Zurich, Universitätstrasse 2, 8092 Zurich, Switzerland, and Functional Genomics Center Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland
* Corresponding author; email: sbaginsky{at}ethz.ch.
We have analyzed proteome dynamics during the light-induced development of rice chloroplasts from etioplasts using quantitative 2-dimensional gel electrophoresis and MS/MS protein identification. In the dark, the etioplast allocates the main proportion of total protein mass to carbohydrate and amino acid metabolism and a surprisingly high number of proteins to the regulation and expression of plastid genes. Chaperones, proteins for photosynthetic energy metabolism, and enzymes of the tetrapyrrole pathway were identified among the most abundant etioplast proteins. The detection of 13 N-terminal acetylated peptides allowed us to map the exact localization of the transit peptide cleavage site, demonstrating a good agreement with the prediction for most proteins. Based on the quantitative etioplast proteome map, we examined early light-induced changes during chloroplast development. The transition from heterotrophic metabolism to photosynthesis-supported autotrophic metabolism was already detectable two hours after illumination and affected most essential metabolic modules. Enzymes in carbohydrate metabolism, photosynthesis and gene expression were up-regulated, while enzymes in amino acid and fatty acid metabolism were significantly decreased in relative abundance. Enzymes involved in nucleotide metabolism, tetrapyrrole biosynthesis and redox regulation remained unchanged. Phosphoprotein-specific staining at different time points during chloroplast development revealed light-induced phosphorylation of a nuclear-encoded plastid RNA binding protein, consistent with changes in plastid RNA metabolism. Quantitative information about all identified proteins and their regulation by light is available in "plprot", the plastid proteome database (http://www.plprot.ethz.ch).
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