The photosystem I supercomplex from a primordial green alga <i>Ostreococcus tauri</i> harbors three light-harvesting complex trimers.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 36951548.
- Also identified by DOI 10.7554/eLife.84488 and PMC identifier 10097422.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
As a ubiquitous picophytoplankton in the ocean and an early-branching green alga, <i>Ostreococcus tauri</i> is a model prasinophyte species for studying the functional evolution of the light-harvesting systems in photosynthesis. Here, we report the structure and function of the <i>O. tauri</i> photosystem I (PSI) supercomplex in low light conditions, where it expands its photon-absorbing capacity by assembling with the light-harvesting complexes I (LHCI) and a prasinophyte-specific light-harvesting complex (Lhcp). The architecture of the supercomplex exhibits hybrid features of the plant-type and the green algal-type PSI supercomplexes, consisting of a PSI core, an Lhca1-Lhca4-Lhca2-Lhca3 belt attached on one side and an Lhca5-Lhca6 heterodimer associated on the other side between PsaG and PsaH. Interestingly, nine Lhcp subunits, including one Lhcp1 monomer with a phosphorylated amino-terminal threonine and eight Lhcp2 monomers, oligomerize into three trimers and associate with PSI on the third side between Lhca6 and PsaK. The Lhcp1 phosphorylation and the light-harvesting capacity of PSI were subjected to reversible photoacclimation, suggesting that the formation of <i>Ot</i>PSI-LHCI-Lhcp supercomplex is likely due to a phosphorylation-dependent mechanism induced by changes in light intensity. Notably, this supercomplex did not exhibit far-red peaks in the 77 K fluorescence spectra, which is possibly due to the weak coupling of the chlorophyll <i>a</i>603-<i>a</i>609 pair in <i>Ot</i>Lhca1-4.
Medical subject headings
- Photosystem I Protein Complex
- Chlorophyta