| Literature DB >> 33051267 |
Tomas E van den Berg1, Rameez Arshad2,3, Wojciech J Nawrocki1, Egbert J Boekema2, Roman Kouřil3, Roberta Croce4.
Abstract
PSI is an essential component of the photosynthetic apparatus of oxygenic photosynthesis. While most of its subunits are conserved, recent data have shown that the arrangement of the light-harvesting complexes I (LHCIs) differs substantially in different organisms. Here we studied the PSI-LHCI supercomplex of Botryococccus braunii, a colonial green alga with potential for lipid and sugar production, using functional analysis and single-particle electron microscopy of the isolated PSI-LHCI supercomplexes complemented by time-resolved fluorescence spectroscopy in vivo. We established that the largest purified PSI-LHCI supercomplex contains 10 LHCIs (∼240 chlorophylls). However, electron microscopy showed heterogeneity in the particles and a total of 13 unique binding sites for the LHCIs around the PSI core. Time-resolved fluorescence spectroscopy indicated that the PSI antenna size in vivo is even larger than that of the purified complex. Based on the comparison of the known PSI structures, we propose that PSI in B. braunii can bind LHCIs at all known positions surrounding the core. This organization maximizes the antenna size while maintaining fast excitation energy transfer, and thus high trapping efficiency, within the complex.Entities:
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Year: 2020 PMID: 33051267 PMCID: PMC7723122 DOI: 10.1104/pp.20.00823
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340