ArticleProceedings of the National Academy of Sciences of the United States of America2016
A repeat protein links Rubisco to form the eukaryotic carbon-concentrating organelle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.
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136 citing papers in PubMed, 281 citations in OpenAlex.
- Transfer of chloroplastSynthetic and systems biotechnology · 2027Article
- Pyrenoid-based CO2-concentrating mechanisms across diverse lineages: convergent features and their applications for engineering.Plant physiology · 2026Review
- Article
- The mosaic of aquatic photorespiration: evolution, diversity, and global biogeochemical impacts.The New phytologist · 2026Review
- EPOS1 is required for normal pyrenoid starch sheath formation and efficiency of the COThe New phytologist · 2026Article
- Bottom-up reconstruction of synthetic pyrenoids provides insights into the mechanisms and evolution of carbon concentration by EPYC1 proteins.Nature plants · 2026Article
- Rapid reconstitution and kinase-controlled regulation of algal pyrenoid condensates in engineeredbioRxiv : the preprint server for biology · 2026Article
- Super-resolution expansion microscopy reveals nanoscale protein domains and CObioRxiv : the preprint server for biology · 2026Article
- RBMP2 shapes specialized membranes for CObioRxiv : the preprint server for biology · 2026Article
- CIA5 and its interacting metal-binding GTPase ZNG3 are degraded by the proteasome in Zn deficiency.The Plant journal : for cell and molecular biology · 2026Article
- Bioengineered algal lipids enriched in structured medium- and long-chain triacylglycerols, linoleate, andbioRxiv : the preprint server for biology · 2026Article
- SAGA1 and SAGA2 localize the starch sheath to the pyrenoid inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Architectural and biochemical advances in understanding microbial COThe Plant journal : for cell and molecular biology · 2026Review
- Kinase KEY1 controls pyrenoid condensate size throughout the cell cycle by disrupting phase separation interactions.Nature cell biology · 2026Article
- Transient molecular chimerism for exploiting xenogeneic organelles.Nature communications · 2026Article
- Partitioning of Rubisco activase into the pyrenoidal Rubisco condensate is mediated by a functional protein-protein interaction.Nature communications · 2026Article
- SAGA1 and SAGA2 localize the starch sheath to the pyrenoid inbioRxiv : the preprint server for biology · 2026Article
- Synthetic Biology of Plants and Microbes for Agriculture, Environment, and Future Applications.Chemical reviews · 2026Review
- Metabolic rewiring and biomass redistribution enable optimized mixotrophic growth in Chlamydomonas.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Proteomic analysis of the pyrenoid-traversing membranes of Chlamydomonas reinhardtii reveals novel components.The New phytologist · 2026Article
76 more citing papers are in PubMed but not listed here.
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19 authors at 7 institutions in 3 countries.
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Abstract
Biological carbon fixation is a key step in the global carbon cycle that regulates the atmosphere's composition while producing the food we eat and the fuels we burn. Approximately one-third of global carbon fixation occurs in an overlooked algal organelle called the pyrenoid. The pyrenoid contains the CO2-fixing enzyme Rubisco and enhances carbon fixation by supplying Rubisco with a high concentration of CO2 Since the discovery of the pyrenoid more that 130 y ago, the molecular structure and biogenesis of this ecologically fundamental organelle have remained enigmatic. Here we use the model green alga Chlamydomonas reinhardtii to discover that a low-complexity repeat protein, Essential Pyrenoid Component 1 (EPYC1), links Rubisco to form the pyrenoid. We find that EPYC1 is of comparable abundance to Rubisco and colocalizes with Rubisco throughout the pyrenoid. We show that EPYC1 is essential for normal pyrenoid size, number, morphology, Rubisco content, and efficient carbon fixation at low CO2 We explain the central role of EPYC1 in pyrenoid biogenesis by the finding that EPYC1 binds Rubisco to form the pyrenoid matrix. We propose two models in which EPYC1's four repeats could produce the observed lattice arrangement of Rubisco in the Chlamydomonas pyrenoid. Our results suggest a surprisingly simple molecular mechanism for how Rubisco can be packaged to form the pyrenoid matrix, potentially explaining how Rubisco packaging into a pyrenoid could have evolved across a broad range of photosynthetic eukaryotes through convergent evolution. In addition, our findings represent a key step toward engineering a pyrenoid into crops to enhance their carbon fixation efficiency.
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