ArticleThe EMBO journal2025
Layered entrenchment maintains essentiality in the evolution of Form I Rubisco complexes.
Article in The EMBO journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Machine learning-assisted directed evolution of plant Rubisco.Science advances · 2026Article
- The fitness landscape of a form II rubisco in a photosynthetic bacterium guides engineering of oxygen tolerance.Science advances · 2026Article
- Rubisco kinetic acclimation at the holoenzyme level.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Evolutionary cell biology comes of age.Journal of cell science · 2025Article
- Electrostatic changes enabled the diversification of an exocyst subunit via protein complex escape.Nature plants · 2025Article
- A Cyanobacterial Screening Platform for Rubisco Mutant Variants.ACS synthetic biology · 2025Article
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Authors and funding
5 authors.
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Abstract
Protein complexes composed of strictly essential subunits are abundant in nature and often arise through the gradual complexification of ancestral precursor proteins. Essentiality can arise through the accumulation of changes that are tolerated in the complex state but would be deleterious for the standalone complex components. While this theoretical framework to explain how essentiality arises has been proposed long ago, it is unclear which factors cause essentiality to persist over evolutionary timescales. In this work we show that the central enzyme of photosynthesis, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), can easily start to depend on a newly recruited interaction partner through multiple, genetically distinct mechanisms that affect stability, solubility, and catalysis. We demonstrate that layering multiple mechanisms of essentiality can lead to its persistence, even if any given mechanism reverts. More broadly, our work highlights that new interaction partners can drastically re-shape which substitutions are tolerated in the proteins they are recruited into. This can lead to the evolution of multilayered essentiality through the exploration of areas of sequence space that are only accessible in the complex state.
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