| Autor: |
Chun S. Lau, Alan K. Itakura, Lianyong Wang, Weronika Patena, Gary Yates, Martin C. Jonikas, Tom Z. Emrich-Mills, Luke C. M. Mackinder, Moritz T. Meyer, Shan He |
| Rok vydání: |
2020 |
| Předmět: |
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| DOI: |
10.1101/2020.08.16.252858 |
| 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 sub-compartments - 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 discovered that pyrenoid proteins share a sequence motif. We show that the motif is 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 sub-compartments together. Our findings advance our understanding of pyrenoid biogenesis and illustrate how a single protein motif can underlie the architecture of a complex multi-layered phase-separated organelle.One Sentence SummaryA ubiquitous Rubisco-binding motif targets proteins to the pyrenoid and holds together the pyrenoid’s three sub-compartments. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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