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Structural Diversity of Photosystem I and Its Light-Harvesting System in Eukaryotic Algae and Plants.

ABSTRACT: Photosystem I (PSI) is one of the most efficient photoelectric apparatus in nature, converting solar energy into condensed chemical energy with almost 100% quantum efficiency. The ability of PSI to attain such high conversion efficiency depends on the precise spatial arrangement of its protein subunits and binding cofactors. The PSI structures of oxygenic photosynthetic organisms, namely cyanobacteria, eukaryotic algae, and plants, have undergone great variation during their evolution, especially in eukaryotic algae and vascular plants for which light-harvesting complexes (LHCI) developed that surround the PSI core complex. A detailed understanding of the functional and structural properties of this PSI-LHCI is not only an important foundation for understanding the evolution of photosynthetic organisms but is also useful for designing future artificial photochemical devices. Recently, the structures of such PSI-LHCI supercomplexes from red alga, green alga, diatoms, and plants were determined by X-ray crystallography and single-particle cryo-electron microscopy (cryo-EM). These findings provide new insights into the various structural adjustments of PSI, especially with respect to the diversity of peripheral antenna systems arising via evolutionary processes. Here, we review the structural details of the PSI tetramer in cyanobacteria and the PSI-LHCI and PSI-LHCI-LHCII supercomplexes from different algae and plants, and then discuss the diversity of PSI-LHCI in oxygenic photosynthesis organisms.

SUBMITTER: Bai T

PROVIDER: S-EPMC8669154 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:BackgroundLight harvesting complex (LHC) proteins function in photosynthesis by binding chlorophyll (Chl) and carotenoid molecules that absorb light and transfer the energy to the reaction center Chl of the photosystem. Most research has focused on LHCs of plants and chlorophytes that bind Chl a and b and extensive work on these proteins has uncovered a diversity of biochemical functions, expression patterns and amino acid sequences. We focus here on a less-studied family of LHCs that typically bind Chl a and c, and that are widely distributed in Chl c-containing and other algae. Previous phylogenetic analyses of these proteins suggested that individual algal lineages possess proteins from one or two subfamilies, and that most subfamilies are characteristic of a particular algal lineage, but genome-scale datasets had revealed that some species have multiple different forms of the gene. Such observations also suggested that there might have been an important influence of endosymbiosis in the evolution of LHCs.ResultsWe reconstruct a phylogeny of LHCs from Chl c-containing algae and related lineages using data from recent sequencing projects to give ~10-fold larger taxon sampling than previous studies. The phylogeny indicates that individual taxa possess proteins from multiple LHC subfamilies and that several LHC subfamilies are found in distantly related algal lineages. This phylogenetic pattern implies functional differentiation of the gene families, a hypothesis that is consistent with data on gene expression, carotenoid binding and physical associations with other LHCs. In all probability LHCs have undergone a complex history of evolution of function, gene transfer, and lineage-specific diversification.ConclusionThe analysis provides a strikingly different picture of LHC diversity than previous analyses of LHC evolution. Individual algal lineages possess proteins from multiple LHC subfamilies. Evolutionary relationships showed support for the hypothesized origin of Chl c plastids. This work also allows recent experimental findings about molecular function to be understood in a broader phylogenetic context.

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Structural Diversity of Photosystem I and Its Light-Harvesting System in Eukaryotic Algae and Plants.

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