ArticleNature plants2021
Structural basis of LhcbM5-mediated state transitions in green algae.
Article in Nature plants, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Structural insights into assembly and environmental adaptation of photosystem I from a lichen green alga.Nature communications · 2026Article
- Roles of LHCSR3 and STT7 in the remodeling of thylakoid supercomplexes in Chlamydomonas reinhardtii under UV-B treatment.The New phytologist · 2026Article
- The amino terminus of PetD is essential for cytochrome bNature plants · 2026Article
- Cryo-EM structural analyses of chlorophyll b-enriched PSI-LHC and PSII-LHC supercomplexes of the siphonous green alga Bryopsis corticulans.Plant communications · 2026Article
- Cryo-EM structure of a photosystem I supercomplex from Euglena gracilis containing pentameric LHCE and dimeric LHCII.Nature communications · 2026Article
- Native alleles at lhcb6 shape photosynthetic efficiency and early growth in maize.Scientific reports · 2026Article
- Structural basis of diadinoxanthin-Chl a/b-binding proteins in the photosystem I supercomplex ofScience advances · 2026Article
- Structure and energy transfer of a far-red-absorbing euglenophyte PSI-LhcE-LhcbM supercomplex.Nature communications · 2026Article
- Molecular architecture for state transition: insights from structural biology and evolutionary trajectories.Plant & cell physiology · 2025Review
- Structure, regulation and assembly of the photosynthetic electron transport chain.Nature reviews. Molecular cell biology · 2025Review
- Too dim, too bright, and just right: Systems analysis of the Chlamydomonas diurnal program under limiting and excess light.The Plant cell · 2025Article
- Biochemical and phylogenetic analyses of light-harvesting complexes from Tetraselmis striata.Photosynthesis research · 2025Article
- X-Ray Crystal and Cryo-Electron Microscopy Structure Analysis Unravels How the Unique Thylakoid Lipid Composition Is Utilized by CytochromeMembranes · 2025Article
- Development of a TSR-based method for understanding structural relationships of cofactors and local environments in photosystem I.BMC bioinformatics · 2025Article
- The future of Asian biophysics built through Korea-Japan collaboration.Biophysics and physicobiology · 2025Article
- Macroscale structural changes of thylakoid architecture during high light acclimation in Chlamydomonas reinhardtii.Photosynthesis research · 2024Article
- Light-Driven HPlants (Basel, Switzerland) · 2024Review
- Regulation of Microalgal Photosynthetic Electron Transfer.Plants (Basel, Switzerland) · 2024Review
- Structure of the red-shifted Fittonia albivenis photosystem I.Nature communications · 2024Article
- Chemical Protein Crosslinking-Coupled Mass Spectrometry Reveals Interaction of LHCI with LHCII and LHCSR3 inPlants (Basel, Switzerland) · 2024Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In green algae and plants, state transitions serve as a short-term light-acclimation process in the regulation of the light-harvesting capacity of photosystems I and II (PSI and PSII, respectively). During the process, a portion of light-harvesting complex II (LHCII) is phosphorylated, dissociated from PSII and binds with PSI to form the supercomplex PSI-LHCI-LHCII. Here, we report high-resolution structures of PSI-LHCI-LHCII from Chlamydomonas reinhardtii, revealing the mechanism of assembly between the PSI-LHCI complex and two phosphorylated LHCII trimers containing all four types of LhcbM protein. Two specific LhcbM isoforms, namely LhcbM1 and LhcbM5, directly interact with the PSI core through their phosphorylated amino terminal regions. Furthermore, biochemical and functional studies on mutant strains lacking either LhcbM1 or LhcbM5 indicate that only LhcbM5 is indispensable in supercomplex formation. The results unravel the specific interactions and potential excitation energy transfer routes between green algal PSI and two phosphorylated LHCIIs.
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