Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
Abstract
Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the fixation of atmospheric CO(2) in photosynthesis, but tends to form inactive complexes with its substrate ribulose 1,5-bisphosphate (RuBP). In plants, Rubisco is reactivated by the AAA(+) (ATPases associated with various cellular activities) protein Rubisco activase (Rca), but no such protein is known for the Rubisco of red algae. Here we identify the protein CbbX as an activase of red-type Rubisco. The 3.0-Å crystal structure of unassembled CbbX from Rhodobacter sphaeroides revealed an AAA(+) protein architecture. Electron microscopy and biochemical analysis showed that ATP and RuBP must bind to convert CbbX into functionally active, hexameric rings. The CbbX ATPase is strongly stimulated by RuBP and Rubisco. Mutational analysis suggests that CbbX functions by transiently pulling the carboxy-terminal peptide of the Rubisco large subunit into the hexamer pore, resulting in the release of the inhibitory RuBP. Understanding Rubisco activation may facilitate efforts to improve CO(2) uptake and biomass production by photosynthetic organisms.
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The Cbbx protein has been identified as an activase of red-type Rubisco.
“The Cbbx protein has been identified as an activase of red-type Rubisco (Mueller-Cajar et al., 2011).”
From Responses of<i>Nannochloropsis oceanica</i>IMET1 to Long-Term Nitrogen Starvation and Recovery (2013) · cites this paper as Mueller-Cajar et al., 2011
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- Authors
- Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F. U., Bracher, A., & Hayer-Hartl, M.
- Affiliations
- Max Planck Institute of Biochemistry (DE)
- Ludwig-Maximilians-Universität München (DE)
- Corresponding author
- Bracher, Andreas
- Hayer-Hartl, Manajit
- Venue
- Nature
- Published
- 2011-11
- Volume
- 479
- Issue
- 7372
- Pages
- 194-199
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1982129514
- Cited by
- 190
- References
- 60
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 7 · 2023: 7 · 2022: 18 · 2021: 12 · 2020: 11 · 2019: 11 · 2018: 12 · 2017: 24 · 2016: 10 · 2015: 15 · 2014: 17 · 2013: 18 · 2012: 6
- FWCI
- 5.84
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- European Synchrotron Radiation Facility
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Keywords
- Rubisco activase, Rubisco, AAA+ ATPase, red algae, Rhodobacter sphaeroides, Rubisco activation, ribulose-1,5-bisphosphate, carboxy-terminal peptide, CO2 fixation, photosynthesis, protein crystal structure
- MeSH terms
- Adenosine Triphosphate, Allosteric Regulation, Bacterial Proteins, Carbon Dioxide, Enzyme Activation, Models, Molecular, Rhodobacter sphaeroides, Ribulose-Bisphosphate Carboxylase, Ribulosephosphates, Structure-Activity Relationship, Crystallography, X-Ray, Protein Structure, Quaternary, Protein Multimerization
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