Assembly of the algal CO 2 -fixing organelle, the pyrenoid, is guided by a Rubisco-binding motif
| Autor: | Alan K. Itakura, Lianyong Wang, Shan He, Tom Z. Emrich-Mills, Chun S. Lau, Weronika Patena, Luke C. M. Mackinder, Moritz T. Meyer, Martin C. Jonikas, Gary Yates |
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| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
0303 health sciences Multidisciplinary biology Chemistry fungi RuBisCO food and beverages Chlamydomonas reinhardtii biology.organism_classification Photosynthesis 01 natural sciences Pyrenoid Cell biology 03 medical and health sciences Organelle biology.protein Sequence motif Structural motif Biogenesis 030304 developmental biology 010606 plant biology & botany |
| Zdroj: | Science Advances. 6 |
| ISSN: | 2375-2548 |
| DOI: | 10.1126/sciadv.abd2408 |
| Popis: | Approximately one-third of the Earth's photosynthetic CO2 assimilation occurs in a pyrenoid, an organelle containing the CO2-fixing enzyme Rubisco. How constituent proteins are recruited to the pyrenoid and how the organelle's subcompartments-membrane tubules, a surrounding phase-separated Rubisco matrix, and a peripheral starch sheath-are held together is unknown. Using the model alga Chlamydomonas reinhardtii, we found that pyrenoid proteins share a sequence motif. We show that the motif is necessary and sufficient to target proteins to the pyrenoid and that the motif binds to Rubisco, suggesting a mechanism for targeting. The presence of the Rubisco-binding motif on proteins that localize to the tubules and on proteins that localize to the matrix-starch sheath interface suggests that the motif holds the pyrenoid's three subcompartments together. Our findings advance our understanding of pyrenoid biogenesis and illustrate how a single protein motif can underlie the architecture of a complex multilayered phase-separated organelle. |
| Databáze: | OpenAIRE |
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