Plant Physiol. Bio-Rad Microplate Reader
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Plant Physiology Preview
Published on December 22, 2006; 10.1104/pp.106.090738

This Article
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow Supplemental Data
Right arrow All Versions of this Article:
143/2/912    most recent
pp.106.090738v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kleffmann, T.
Right arrow Articles by Baginsky, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kleffmann, T.
Right arrow Articles by Baginsky, S.
Agricola
Right arrow Articles by Kleffmann, T.
Right arrow Articles by Baginsky, S.

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).




This article has been cited by other articles:


Home page
 Molecular Cancer TherapeuticsHome page
M. Sedic, M. Poznic, P. Gehrig, M. Scott, R. Schlapbach, M. Hranjec, G. Karminski-Zamola, K. Pavelic, and S. K. Pavelic
Differential antiproliferative mechanisms of novel derivative of benzimidazo[1,2-{alpha}]quinoline in colon cancer cells depending on their p53 status
Mol. Cancer Ther., July 1, 2008; 7(7): 2121 - 2132.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
T. Aki, M. Shigyo, R. Nakano, T. Yoneyama, and S. Yanagisawa
Nano Scale Proteomics Revealed the Presence of Regulatory Proteins Including Three FT-Like proteins in Phloem and Xylem Saps from Rice
Plant Cell Physiol., May 1, 2008; 49(5): 767 - 790.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
E. Kanervo, M. Singh, M. Suorsa, V. Paakkarinen, E. Aro, N. Battchikova, and E.-M. Aro
Expression of Protein Complexes and Individual Proteins Upon Transition of Etioplasts to Chloroplasts in Pea (Pisum sativum)
Plant Cell Physiol., March 1, 2008; 49(3): 396 - 410.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 2006 by the American Society of Plant Biologists