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Eukaryotic Cell, October 2003, p. 978-994, Vol. 2, No. 5
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.5.978-994.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Proteomics of Chlamydomonas reinhardtii Light-Harvesting Proteins

Einar J. Stauber,1 Andreas Fink,1 Christine Markert,1 Olaf Kruse,2 Udo Johanningmeier,3 and Michael Hippler1*

Lehrstuhl für Pflanzenphysiologie, Friedrich-Schiller-Universität Jena, 07743 Jena,1 Molekulare Zellphysiologie, Universität Bielefeld, 33501 Bielefeld,2 Institut für Pflanzenphysiologie, Martin-Luther-Universität Halle-Wittenberg, 06120 Halle, Germany3

Received 28 February 2003/ Accepted 21 June 2003

With the recent development of techniques for analyzing transmembrane thylakoid proteins by two-dimensional gel electrophoresis, systematic approaches for proteomic analyses of membrane proteins became feasible. In this study, we established detailed two-dimensional protein maps of Chlamydomonas reinhardtii light-harvesting proteins (Lhca and Lhcb) by extensive tandem mass spectrometric analysis. We predicted eight distinct Lhcb proteins. Although the major Lhcb proteins were highly similar, we identified peptides which were unique for specific lhcbm gene products. Interestingly, lhcbm6 gene products were resolved as multiple spots with different masses and isoelectric points. Gene tagging experiments confirmed the presence of differentially N-terminally processed Lhcbm6 proteins. The mass spectrometric data also revealed differentially N-terminally processed forms of Lhcbm3 and phosphorylation of a threonine residue in the N terminus. The N-terminal processing of Lhcbm3 leads to the removal of the phosphorylation site, indicating a potential novel regulatory mechanism. At least nine different lhca-related gene products were predicted by comparison of the mass spectrometric data against Chlamydomonas expressed sequence tag and genomic databases, demonstrating the extensive variability of the C. reinhardtii Lhca antenna system. Out of these nine, three were identified for the first time at the protein level. This proteomic study demonstrates the complexity of the light-harvesting proteins at the protein level in C. reinhardtii and will be an important basis of future functional studies addressing this diversity.

* Corresponding author. Mailing address: Lehrstuhl für Pflanzenphysiologie, Friedrich-Schiller-Universität Jena, Dornburger Str. 159, 07743 Jena, Germany. Phone: 49 3641949237. Fax: 49 3641949232. E-mail: m.hippler{at}uni-jena.de.

Eukaryotic Cell, October 2003, p. 978-994, Vol. 2, No. 5
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.5.978-994.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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