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    1. Plant Biology
    2. Structural Biology and Molecular Biophysics

    Structure of Dunaliella photosystem II reveals conformational flexibility of stacked and unstacked supercomplexes

    Ido Caspy, Maria Fadeeva ... Nathan Nelson
    Photosystem II, the pigment-protein complex responsible for water oxidation in photosynthesis, was found to exist in two different core conformations with altered antennae connectivity.
    1. Biochemistry and Chemical Biology
    2. Evolutionary Biology

    Comprehensive phylogenetic analysis of the ribonucleotide reductase family reveals an ancestral clade

    Audrey A Burnim, Matthew A Spence ... Nozomi Ando
    A large-scale phylogenetic inference of the ribonucleotide reductase family reveals a new distinct clade with implications on how nature adapted to environmental changes.
    1. Plant Biology
    2. Structural Biology and Molecular Biophysics

    Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus

    Koji Kato, Tasuku Hamaguchi ... Jian-Ren Shen
    Primordial cyanobacterial PSI structure.
    1. Plant Biology

    A guanosine tetraphosphate (ppGpp) mediated brake on photosynthesis is required for acclimation to nitrogen limitation in Arabidopsis

    Shanna Romand, Hela Abdelkefi ... Ben Field
    Guanosine tetraphosphate (ppGpp) is a pivotal regulator of chloroplast activity that is required for acclimation to nitrogen limitation in the model plant Arabidopsis.
    1. Biochemistry and Chemical Biology
    2. Evolutionary Biology

    Pyruvate:ferredoxin oxidoreductase and low abundant ferredoxins support aerobic photomixotrophic growth in cyanobacteria

    Yingying Wang, Xi Chen ... Kirstin Gutekunst
    Synechocystis switches its redox pools under reducing photomixotrophic conditions from utilizing NAD(H)- to ferredoxin-dependent enzymes and thereby balances its metabolism in a trade-off between energy conservation and chemical driving forces.
    1. Biochemistry and Chemical Biology

    Cooperation among c-subunits of FoF1-ATP synthase in rotation-coupled proton translocation

    Noriyo Mitome, Shintaroh Kubo ... Shoji Takada
    Biochemical analysis on hetero-mutated c10 subunits ring and molecular dynamics simulations demonstrate the cooperation among c-subunits of FoF1-ATP synthase in rotation-coupled proton translocation.
    1. Biochemistry and Chemical Biology
    2. Plant Biology

    The induction of pyrenoid synthesis by hyperoxia and its implications for the natural diversity of photosynthetic responses in Chlamydomonas

    Peter Neofotis, Joshua Temple ... David M Kramer
    The algal pyrenoid is formed at high O2 levels, even when CO2 is high, implying that a product of photosynthesis, most likely H2O2 acts as a signal.
    1. Cell Biology
    2. Plant Biology

    Crosstalk between the chloroplast protein import and SUMO systems revealed through genetic and molecular investigation in Arabidopsis

    Samuel James Watson, Na Li ... R Paul Jarvis
    The small ubiquitin-like modifier system directly regulates components of the chloroplast protein import apparatus, that is, TOC proteins, to control chloroplast biogenesis and plant development.
    1. Plant Biology
    2. Structural Biology and Molecular Biophysics

    In situ cryo-ET structure of phycobilisome–photosystem II supercomplex from red alga

    Meijing Li, Jianfei Ma ... Sen-Fang Sui
    The nature of the phycobilisome–photosystem II supercomplex on the native thylakoid determined with cryo-electron tomography at an unprecedented resolution reveals that one phycobilisome interconnects with six photosystem monomers.
    1. Plant Biology
    2. Structural Biology and Molecular Biophysics

    The structure of photosystem I from a high-light-tolerant cyanobacteria

    Zachary Dobson, Safa Ahad ... Yuval Mazor
    The necessity of studying extremophile organisms is exemplified by the structure of photosystem I from a high-light tolerant cyanobacteria, demonstrating the relationship between the structure and function in photosystem I.