ArticleCurrent biology : CB2023
Deep-branching evolutionary intermediates reveal structural origins of form I rubisco.
Article in Current biology : CB, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Diversity-driven biochemical survey reveals widespread dimerization throughout the rubisco superfamily.Nature communications · 2026Article
- Rubisco kinetic acclimation at the holoenzyme level.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Autotrophic growth ofFrontiers in microbiology · 2026Article
- Exploring the Diversity and Metabolic Potential of COMicrobes and environments · 2026Article
- High-resolution structure of the heat-stable form-IAq RuBisCO from the thermophilic purple sulfur bacterium Thermochromatium tepidum.Scientific reports · 2025Article
- Chemoautotrophy in subzero environments and the potential for cold-adapted Rubisco.Applied and environmental microbiology · 2025Article
- Comprehensive Insights into Potential Metabolic Functions of Myxococcota in Activated Sludge Systems.Microbes and environments · 2024Article
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Authors and funding
12 authors at 6 institutions in 4 countries.
Funding
Abstract
The enzyme rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyzes the majority of biological carbon fixation on Earth. Although the vast majority of rubiscos across the tree of life assemble as homo-oligomers, the globally predominant form I enzyme-found in plants, algae, and cyanobacteria-forms a unique hetero-oligomeric complex. The recent discovery of a homo-oligomeric sister group to form I rubisco (named form I') has filled a key gap in our understanding of the enigmatic origins of the form I clade. However, to elucidate the series of molecular events leading to the evolution of form I rubisco, we must examine more distantly related sibling clades to contextualize the molecular features distinguishing form I and form I' rubiscos. Here, we present a comparative structural study retracing the evolutionary history of rubisco that reveals a complex structural trajectory leading to the ultimate hetero-oligomerization of the form I clade. We structurally characterize the oligomeric states of deep-branching form Iα and I'' rubiscos recently discovered from metagenomes, which represent key evolutionary intermediates preceding the form I clade. We further solve the structure of form I'' rubisco, revealing the molecular determinants that likely primed the enzyme core for the transition from a homo-oligomer to a hetero-oligomer. Our findings yield new insight into the evolutionary trajectory underpinning the adoption and entrenchment of the prevalent assembly of form I rubisco, providing additional context when viewing the enzyme family through the broader lens of protein evolution.
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