Cell-free reconstitution reveals centriole cartwheel assembly mechanisms.

Guichard, P; Hamel, V; Le Guennec, M; Banterle, N; Iacovache, Mircea Ioan; Nemčíková, V; Flückiger, I; Goldie, K N; Stahlberg, H; Lévy, D; Zuber, Benoît; Gönczy, P (2017). Cell-free reconstitution reveals centriole cartwheel assembly mechanisms. Nature communications, 8(14813), p. 14813. Nature Publishing Group 10.1038/ncomms14813

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How cellular organelles assemble is a fundamental question in biology. The centriole organelle organizes around a nine-fold symmetrical 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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