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Cell-free reconstitution reveals centriole cartwheel assembly mechanisms.

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Guichard P, Hamel V, Le Guennec M, Banterle N, Iacovache I, Nemčíková V, Flückiger I, Goldie K N, Stahlberg H, Lévy D, Zuber B, Gönczy P,
Project Time-resolved structural study of calcium-dependent membrane fusion
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Original article (peer-reviewed)

Journal Nature communications
Volume (Issue) 8
Page(s) 14813 - 14813
Title of proceedings Nature communications
DOI 10.1038/ncomms14813

Open Access

URL https://doi.org/10.1038/ncomms14813
Type of Open Access Publisher (Gold Open Access)

Abstract

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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