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Showing 1–10 of 10 results
Advanced filters: Author: Oliver Mueller-Cajar Clear advanced filters

  • The enzyme Rubisco has a central role in atmospheric CO2 fixation. Rubisco can be inactivated if its sugar substrate is bound prior to carbamylation of a residue in the active site. The structure of tobacco Rca, the enzyme that removes the bound sugar substrate and activates Rubisco, is now presented, offering insight into this process.

    • Mathias Stotz
    • Oliver Mueller-Cajar
    • Manajit Hayer-Hartl
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 1366-1370

  • The second Keystone Symposium on AAA+ proteins, “AAA+ Proteins: From Atomic Structures to Organisms”, was held in Tahoe City, USA in January 2020. The program highlighted recent advances from structural, biochemical and cellular approaches that have extended our understanding of these important ATP-driven molecular machines.

    • Steven E. Glynn
    • Julia R. Kardon
    • Carol Cho
    News & Views
    Nature Structural & Molecular Biology
    Volume: 27, P: 515-518

  • A massively parallel assay developed to map the essential photosynthetic enzyme rubisco showed that non-trivial biochemical changes and improvements in CO2 affinity are possible, signposting further enzyme engineering efforts to increase crop yields.

    • Noam Prywes
    • Naiya R. Phillips
    • David F. Savage
    ResearchOpen Access
    Nature
    Volume: 638, P: 823-828

  • 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
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-10

  • 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
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-10

  • The structural basis of the interactions between Rubisco and its intrinsically disordered linker protein provides insight into phase separation within the algal pyrenoid, an organelle responsible for around a third of global CO2 fixation.

    • Shan He
    • Hui-Ting Chou
    • Martin C. Jonikas
    Research
    Nature Plants
    Volume: 6, P: 1480-1490

  • Plants’ photosynthetic capacity at high light is limited by the kinetics of the slow, carbon-dioxide-fixing enzyme Rubisco. Increasing Rubisco content in a C4 crop plant is now shown to enhance photosynthesis and growth.

    • Oliver Mueller-Cajar
    News & Views
    Nature Plants
    Volume: 4, P: 746-747

  • Although nonspecific chaperones such as GroEL can increase evolvability by helping slightly destabilized mutants, a dedicated assembly chaperone decreases evolvability of the CO2 fixation enzyme Rubisco, providing insights into Rubisco's poor catalytic power.

    • Paulo Durão
    • Harald Aigner
    • Manajit Hayer-Hartl
    Research
    Nature Chemical Biology
    Volume: 11, P: 148-155