ArticleNature communications2015
Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 94 citations in OpenAlex.
- NorQD AAA+ complex drives metal insertion by a twisting mechanism.Nature communications · 2026Article
- Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction.Nature communications · 2026Article
- Recent insights into α-carboxysome structure, mechanism, and assembly.Journal of bacteriology · 2026Review
- Host species-specific gene expression by a widespread and flexible chemosynthetic symbiont.The ISME journal · 2026Article
- Structural modeling and biochemical characterization of MSMEG_0748, a MoxR ATPase fromComputational and structural biotechnology journal · 2025Article
- Molecular principles of the assembly and construction of a carboxysome shell.Science advances · 2024Article
- Cyanobacterial α-carboxysome carbonic anhydrase is allosterically regulated by the Rubisco substrate RuBP.Science advances · 2024Article
- Identification of a carbonic anhydrase-Rubisco complex within the alpha-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Engineering α-carboxysomes into plant chloroplasts to support autotrophic photosynthesis.Nature communications · 2023Article
- Article
- Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling.Frontiers in molecular biosciences · 2023Review
- Decoding the Absolute Stoichiometric Composition and Structural Plasticity of α-Carboxysomes.mBio · 2022Article
- The MIDAS domain of AAA mechanoenzyme Mdn1 forms catch bonds with two different substrates.eLife · 2022Article
- Incorporation of Functional Rubisco Activases into Engineered Carboxysomes to Enhance Carbon Fixation.ACS synthetic biology · 2022Article
- CAM Models: Lessons and Implications for CAM Evolution.Frontiers in plant science · 2022Review
- Enhancing crop yield by using Rubisco activase to improve photosynthesis under elevated temperatures.Stress biology · 2021Review
- Anaerobic Sulfur Oxidation Underlies Adaptation of a Chemosynthetic Symbiont to Oxic-Anoxic Interfaces.mSystems · 2021Article
- New discoveries expand possibilities for carboxysome engineering.Current opinion in microbiology · 2021Review
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) is responsible for almost all biological CO2 assimilation, but forms inhibited complexes with its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. The distantly related AAA+ proteins rubisco activase and CbbX remodel inhibited rubisco complexes to effect inhibitor release in plants and α-proteobacteria, respectively. Here we characterize a third class of rubisco activase in the chemolithoautotroph Acidithiobacillus ferrooxidans. Two sets of isoforms of CbbQ and CbbO form hetero-oligomers that function as specific activases for two structurally diverse rubisco forms. Mutational analysis supports a model wherein the AAA+ protein CbbQ functions as motor and CbbO is a substrate adaptor that binds rubisco via a von Willebrand factor A domain. Understanding the mechanisms employed by nature to overcome rubisco's shortcomings will increase our toolbox for engineering photosynthetic carbon dioxide fixation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.