Proteotypic profiling of LHCI from Chlamydomonas reinhardtii provides new insights into structure and function of the complex |
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Authors: | Einar J Stauber Andreas Busch Bianca Naumann Ale? Svato? Michael Hippler Professor |
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Institution: | 1. Mass Spectrometry Group, Max Planck Institute for Chemical Ecology, Jena, Germany;2. Current address: Institut für Pharmazeutische Biologie, Technische Universit?t Braunschweig, Mendelssohnstr. 1, 38106 Braunschweig, Germany.;3. Both authors contributed equally to this work.;4. Institut für Biochemie und Biotechnologie der Pflanzen, Westf?lische Wilhelms‐Universit?t, Münster, Germany |
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Abstract: | We used isotope dilution MS to measure the stoichiometry of light‐harvesting complex I (LHCI) proteins with the photosystem I (PSI) core complex in the green alga Chlamydomonas reinhardtii. Proteotypic peptides served as quantitative markers for each of the nine gene products (Lhca1–9) and for PSI subunits. The quantitative data revealed that the LHCI antenna of C. reinhardtii contains about 7.5 ± 1.4 subunits. It further demonstrated that the thylakoid LHCI population is heterogeneously composed and that several lhca gene products are not present in 1:1 stoichiometries with PSI. When compared with vascular plants, LHCI of C. reinhardtii possesses a lower proportion of proteins potentially contributing to far‐red fluorescence emission. In general, the strategy presented is universally applicable for exploring subunit stoichiometries within the C. reinhardtii proteome. |
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Keywords: | Membrane proteins Quantitative analysis Stable isotope labelling |
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