Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms14813
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Funding
- Swiss National Science Foundation (SNSF) [PP00P3_157517, SNSF PP00P3_139098, PP00P3_163761]
- Microscopy Imaging Center (MIC) of the University of Bern (FEI Tecnai F20)
- European Research Council [AdG 340227]
- Swiss National Science Foundation (SNF) [PP00P3_157517, PP00P3_163761] Funding Source: Swiss National Science Foundation (SNF)
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How cellular organelles assemble is a fundamental question in biology. The centriole organelle organizes around a nine-foldsymmetrical cartwheel structure typically 100 nm high comprising a stack of rings that each accommodates nine homodimers of SAS-6 proteins. Whether nine- fold symmetrical ring-like assemblies of SAS-6 proteins harbour more peripheral cartwheel elements is unclear. Furthermore, the mechanisms governing ring stacking are not known. Here we develop a cell-free reconstitution system for core cartwheel assembly. Using cryo-electron tomography, we uncover that the Chlamydomonas reinhardtii proteins CrSAS-6 and Bld10p together drive assembly of the core cartwheel. Moreover, we discover that CrSAS-6 possesses autonomous properties that ensure self-organized ring stacking. Mathematical fitting of reconstituted cartwheel height distribution suggests a mechanism whereby preferential addition of pairs of SAS- 6 rings governs cartwheel growth. In conclusion, we have developed a cell-free reconstitution system that reveals fundamental assembly principles at the root of centriole biogenesis.
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