Rubisco articles within Nature Communications

Featured

  • Article
    | Open Access

    Rubisco is responsible for sequestering virtually all of the carbon dioxide in the global carbon cycle. Here, the authors demonstrate that two conserved phosphatases degrade Rubisco misfire products that inhibit photosynthesis in plants.

    • Dario Leister
    • , Anurag Sharma
    •  & Thilo Rühle

  • Article
    | Open Access

    Photosynthesis declines at mild temperatures in terrestrial plants. Here, the authors use published data to show that decline in photosynthetic CO2 assimilation rate with rising temperatures can be accounted for by Rubisco deactivation and declines in chloroplast electron transport rate.

    • Andrew P. Scafaro
    • , Bradley C. Posch
    •  & Owen K. Atkin

  • Article
    | Open Access

    Carboxysomes are bacterial microcompartments encapsulating Rubisco and carbonic anhydrase for carbon fixation. Here, authors determine the organization of Rubisco and its interaction with the linker protein CsoS2 within two distant α-carboxysomes.

    • Tao Ni
    • , Yaqi Sun
    •  & Peijun Zhang

  • Article
    | Open Access

    The fraction of leaf nitrogen allocated to RuBisCO indicates differing nitrogen use strategies of plants and varies considerably. Here the authors show that this variation is largely driven by leaf thickness and phosphorus content with light intensity, atmospheric dryness and soil pH also having considerable influence.

    • Xiangzhong Luo
    • , Trevor F. Keenan
    •  & Yao Zhang

  • Article
    | Open Access

    Introducing the pyrenoid-based CO2-concentrating mechanism of green algae into crops could greatly improve photosynthesis. Here, the authors show that expression of the algal linker protein EPYC1 and a plant-algal hybrid Rubisco in Arabidopsis chloroplasts leads to formation of a phase separated algal-like proto-pyrenoid.

    • Nicky Atkinson
    • , Yuwei Mao
    •  & Alistair J. McCormick

  • Article
    | Open Access

    The microalgal pyrenoid has been reported to behave as a phase-separated liquid compartment. Here the authors demonstrate that the CO2-fixing enzyme Rubisco and the linker protein EPYC1 are necessary and sufficient to bring about a liquid-liquid phase separation that recapitulates the pyrenoid’s liquid-like behavior.

    • Tobias Wunder
    • , Steven Le Hung Cheng
    •  & Oliver Mueller-Cajar

  • Article
    | Open Access

    Previous efforts to assemble Rubisco within a cyanobacterial carboxysome-derived protein shell in plant chloroplasts to concentrate CO2 have been unsuccessful. Here, Long et al. produce carboxysomes in tobacco chloroplasts that encapsulate the introduced Rubisco and enable autotrophic growth at elevated CO2.

    • Benedict M. Long
    • , Wei Yih Hee
    •  & G. Dean Price

  • Article
    | Open Access

    The CO2-fixing enzyme rubisco requires motor proteins known as rubisco activases to remove inhibitors bound to its active site. Here the authors describe a new class of rubisco activase present in chemoautotrophic bacteria that belongs to the MoxR family of AAA+ ATPases.

    • Yi-Chin Candace Tsai
    • , Maria Claribel Lapina
    •  & Oliver Mueller-Cajar

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