Author
Listed:
- P. Guichard
(Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, Swiss Federal Institute of Technology (EPFL)
Present address: Department of Cell Biology, Sciences III, University of Geneva, Geneva CH-1211, Switzerland)
- V. Hamel
(Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, Swiss Federal Institute of Technology (EPFL)
Present address: Department of Cell Biology, Sciences III, University of Geneva, Geneva CH-1211, Switzerland)
- M. Le Guennec
(Sciences III, University of Geneva)
- N. Banterle
(Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, Swiss Federal Institute of Technology (EPFL))
- I. Iacovache
(Institute of Anatomy, University of Bern)
- V. Nemčíková
(Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, Swiss Federal Institute of Technology (EPFL))
- I. Flückiger
(Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, Swiss Federal Institute of Technology (EPFL))
- K. N. Goldie
(Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel)
- H. Stahlberg
(Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel)
- D. Lévy
(Institut Curie, PSL Research University, UMR 168, Centre de Recherche, 26 rue d’ULM, Paris 75231, France)
- B. Zuber
(Institute of Anatomy, University of Bern)
- P. Gönczy
(Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, Swiss Federal Institute of Technology (EPFL))
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.
Suggested Citation
P. Guichard & V. Hamel & M. Le Guennec & N. Banterle & I. Iacovache & V. Nemčíková & I. Flückiger & K. N. Goldie & H. Stahlberg & D. Lévy & B. Zuber & P. Gönczy, 2017.
"Cell-free reconstitution reveals centriole cartwheel assembly mechanisms,"
Nature Communications, Nature, vol. 8(1), pages 1-9, April.
Handle:
RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14813
DOI: 10.1038/ncomms14813
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