Journal
SCIENCE ADVANCES
Volume 6, Issue 46, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.abd2408
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Funding
- NSF [IOS-1359682, MCB-1935444]
- NIH [DP2-GM-119137]
- Simons Foundation
- Howard Hughes Medical Institute [55108535]
- UK Biotechnology and Biological Sciences Research Council [BB/R001014/1]
- BBSRC [BB/R506485/1, BB/S015337/1, BB/R001014/1] Funding Source: UKRI
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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.
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