ArticleNature2010
Coupled chaperone action in folding and assembly of hexadecameric Rubisco.
Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
91 citing papers in PubMed.
- Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026Review
- Effects of light intensity on the growth and photosynthetic physiology of Zelkova schneideriana seedlings.BMC plant biology · 2026Article
- Stages of biomolecular condensate formation in pro-β-carboxysome assembly.Nature plants · 2026Article
- High-Throughput Detection of Cyanobacterial Form I Rubisco Assembly.ACS synthetic biology · 2026Article
- Not just Rubisco: integrated strategies to overcome the biochemical limitations of CFrontiers in plant science · 2026Review
- Targeted genetic manipulation and yeast-like evolutionary genomics in the green alga Auxenochlorella.The Plant cell · 2025Article
- Targeted genetic manipulation and yeast-like evolutionary genomics in the green algabioRxiv : the preprint server for biology · 2025Article
- Directed evolution of a plant Rubisco chaperone with altered client recognition.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Replacement of large subunit N terminus enabled biogenesis of different plant Rubiscos in E. coli.Plant biotechnology journal · 2025Article
- Engineering COPlant communications · 2025Article
- Review
- Evolutionary Dynamics of RuBisCO: Emergence of the Small Subunit and its Impact Through Time.Molecular biology and evolution · 2025Article
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- A systematic exploration of bacterial form I rubisco maximal carboxylation rates.The EMBO journal · 2024Article
- Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Engineering Rubisco to enhance COSynthetic and systems biotechnology · 2024Review
- RNA-dependent proteome solubility maintenance inRNA biology · 2024Article
- Red Rubiscos and opportunities for engineering green plants.Journal of experimental botany · 2023Review
- Phase Separation of Rubisco by the Folded SSUL Domains of CcmM in Beta-Carboxysome Biogenesis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX.Cell discovery · 2022Article
31 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Form I Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase), a complex of eight large (RbcL) and eight small (RbcS) subunits, catalyses the fixation of atmospheric CO(2) in photosynthesis. The limited catalytic efficiency of Rubisco has sparked extensive efforts to re-engineer the enzyme with the goal of enhancing agricultural productivity. To facilitate such efforts we analysed the formation of cyanobacterial form I Rubisco by in vitro reconstitution and cryo-electron microscopy. We show that RbcL subunit folding by the GroEL/GroES chaperonin is tightly coupled with assembly mediated by the chaperone RbcX(2). RbcL monomers remain partially unstable and retain high affinity for GroEL until captured by RbcX(2). As revealed by the structure of a RbcL(8)-(RbcX(2))(8) assembly intermediate, RbcX(2) acts as a molecular staple in stabilizing the RbcL subunits as dimers and facilitates RbcL(8) core assembly. Finally, addition of RbcS results in RbcX(2) release and holoenzyme formation. Specific assembly chaperones may be required more generally in the formation of complex oligomeric structures when folding is closely coupled to assembly.
Indexed as
Identifiers
20075914What OpenQuestion holds
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.