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Eukaryotic Cell, March 2006, p. 457-468, Vol. 5, No. 3
1535-9778/06/$08.00+0     doi:10.1128/EC.5.3.457-468.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Analysis of the Phosphoproteome of Chlamydomonas reinhardtii Provides New Insights into Various Cellular Pathways{dagger}

Volker Wagner,1 Gunther Geßner,1 Ines Heiland,1 Marc Kaminski,1 Susan Hawat,1 Kai Scheffler,2 and Maria Mittag1*

Institut für Allgemeine Botanik, Friedrich-Schiller-Universität Jena, Am Planetarium 1, 07743 Jena,1 Thermo Electron GmbH, Im Steingrund 4-6, 63303 Dreieich, Germany2

Received 6 November 2005/ Accepted 20 December 2005

The unicellular flagellated green alga Chlamydomonas reinhardtii has emerged as a model organism for the study of a variety of cellular processes. Posttranslational control via protein phosphorylation plays a key role in signal transduction, regulation of gene expression, and control of metabolism. Thus, analysis of the phosphoproteome of C. reinhardtii can significantly enhance our understanding of various regulatory pathways. In this study, we have grown C. reinhardtii cultures in the presence of an inhibitor of Ser/Thr phosphatases to increase the phosphoprotein pool. Phosphopeptides from these cells were enriched by immobilized metal-ion affinity chromatography and analyzed by nano-liquid chromatography-electrospray ionization-mass spectrometry (MS) with MS-MS as well as neutral-loss-triggered MS-MS-MS spectra. In this way, we were able to identify 360 phosphopeptides from 328 different phosphoproteins of C. reinhardtii, thus providing new insights into a variety of cellular processes, including metabolic and signaling pathways. Comparative analysis of the phosphoproteome also yielded new functional information on proteins controlled by redox regulation (thioredoxin target proteins) and proteins of the chloroplast 70S ribosome, the centriole, and especially the flagella, for which 32 phosphoproteins were identified. The high yield of phosphoproteins of the latter correlates well with the presence of several flagellar kinases and indicates that phosphorylation/dephosphorylation represents one of the key regulatory mechanisms of eukaryotic cilia. Our data also provide new insights into certain cilium-related mammalian diseases.

* Corresponding author. Mailing address: Institut für Allgemeine Botanik, Friedrich-Schiller-Universität Jena, Am Planetarium 1, 07743 Jena, Germany. Phone: 49 3641 949 201. Fax: 49 3641 949 202. E-mail: M.Mittag{at}uni-jena.de.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, March 2006, p. 457-468, Vol. 5, No. 3
1535-9778/06/$08.00+0     doi:10.1128/EC.5.3.457-468.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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