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Proteotypic profiling of LHCI from Chlamydomonas reinhardtii provides new insights into structure and function of the complex
Author(s) -
Stauber Einar J.,
Busch Andreas,
Naumann Bianca,
Svatoš Aleš,
Hippler Michael
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700620
Subject(s) - chlamydomonas reinhardtii , photosystem i , thylakoid , protein subunit , photosystem ii , proteome , biology , fluorescence , photosynthesis , biophysics , chemistry , biochemistry , gene , chloroplast , physics , quantum mechanics , mutant
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.