Rubisco articles from across Nature Portfolio

The carbon fixation machinery α-carboxysome of the marine cyanobacterium Prochlorococcus is composed of an icosahedral-like proteinaceous shell that encapsulates the enzymes RuBisCO and carbonic anhydrase. Our cryo-EM structure reveals how thousands of protein components self-assemble into the α-carboxysome and characterizes the multivalent interactions by which the scaffolding protein CsoS2 crosslinks the shell with internal RuBisCO molecules.

The cryo-EM structure shows us how thousands of protein components self-assemble into Prochlorococcus α-carboxysome. The scaffolding protein CsoS2 crosslinks the icosahedral-like shell and internal RuBisCOs, and determines the size of α-carboxysome.

To advance crop productivity improvement efforts, the authors integrated crystal structure-guided changes from a highly effective red algae Rubisco into a related bacterial enzyme to improve its CO₂-fixing traits that, in tobacco, enhanced photosynthesis and growth.

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.

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.

Engineering carboxysomes into crop chloroplasts is a potential route to improve photosynthesis and crop yield. Here, the authors engineer functional CO₂-fixing modules into tobacco chloroplasts to improve their photosynthesis and productivity.

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.

The carbon fixation machinery α-carboxysome of the marine cyanobacterium Prochlorococcus is composed of an icosahedral-like proteinaceous shell that encapsulates the enzymes RuBisCO and carbonic anhydrase. Our cryo-EM structure reveals how thousands of protein components self-assemble into the α-carboxysome and characterizes the multivalent interactions by which the scaffolding protein CsoS2 crosslinks the shell with internal RuBisCO molecules.

Guillaume Tcherkez recounts the hard choices of RuBisCo, the most abundant enzyme on Earth.

New capabilities for assembling plant Rubisco in bacteria offer a revolution for enhancing photosynthesis. The technology provides a breakthrough to identify and test solutions for improving CO₂ fixation by crop Rubisco.

Photosynthesis in C₃ plants is limited by the kinetics of the CO₂-fixing enzyme Rubisco. Natural variation in Rubisco can be exploited to provide new avenues for adapting photosynthetic performance to a changing climate while reducing the environmental footprint of agriculture.

Rubisco catalyses the first step in photosynthetic carbon fixation, but it can be easily poisoned by side-products of its activity. Structural and functional analyses of a protein conserved across plants, algae and bacteria shows how one such blockage is both removed and recycled.