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Eukaryotic Cell, July 2009, p. 922-932, Vol. 8, No. 7
1535-9778/09/$08.00+0     doi:10.1128/EC.00067-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Analysis of Flagellar Phosphoproteins from Chlamydomonas reinhardtii{triangledown} ,{dagger}

Jens Boesger,{ddagger} Volker Wagner,{ddagger} Wolfram Weisheit, and Maria Mittag*

Institut für Allgemeine Botanik und Pflanzenphysiologie, Friedrich-Schiller-Universität Jena, Am Planetarium 1, 07743 Jena, Germany

Received 1 March 2009/ Accepted 21 April 2009

Cilia and flagella are cell organelles that are highly conserved throughout evolution. For many years, the green biflagellate alga Chlamydomonas reinhardtii has served as a model for examination of the structure and function of its flagella, which are similar to certain mammalian cilia. Proteome analysis revealed the presence of several kinases and protein phosphatases in these organelles. Reversible protein phosphorylation can control ciliary beating, motility, signaling, length, and assembly. Despite the importance of this posttranslational modification, the identities of many ciliary phosphoproteins and knowledge about their in vivo phosphorylation sites are still missing. Here we used immobilized metal affinity chromatography to enrich phosphopeptides from purified flagella and analyzed them by mass spectrometry. One hundred forty-one phosphorylated peptides were identified, belonging to 32 flagellar proteins. Thereby, 126 in vivo phosphorylation sites were determined. The flagellar phosphoproteome includes different structural and motor proteins, kinases, proteins with protein interaction domains, and many proteins whose functions are still unknown. In several cases, a dynamic phosphorylation pattern and clustering of phosphorylation sites were found, indicating a complex physiological status and specific control by reversible protein phosphorylation in the flagellum.

* Corresponding author. Mailing address: Institute of General Botany and Plant Physiology, Friedrich-Schiller-University Jena, 07743 Jena, Germany. Phone: 49-(0)3641-949-201. Fax: 49-(0)3641-949-202. E-mail: M.Mittag{at}uni-jena.de

{triangledown} Published ahead of print on 8 May 2009.

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

{ddagger} J.B. and V.W. contributed equally to this work.

Eukaryotic Cell, July 2009, p. 922-932, Vol. 8, No. 7
1535-9778/09/$08.00+0     doi:10.1128/EC.00067-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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