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bioRxiv · 10.1101/442590

Electron Cryo-Tomography Provides Insight into Procentriole Architecture and Assembly Mechanism

Li, S.·Fernandez, J.-J.·Marshall, W.·Agard, D.
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Abstract

Centriole is an essential structure with multiple functions in cellular processes. Centriole biogenesis and homeostasis is tightly regulated. Using electron cryo-tomography (cryoET) we present the structure of procentrioles from Chlamydomonas reinhardtii. We identified a set of non-tubulin components attached to the triplet microtubule (MT), many are at the junctions of tubules likely to reinforce the triplet. We describe structure of the A-C linker that bridges neighboring triplets. We find that POC1 is an integral component of the A-C linker. Its conserved WD40 {beta}-propeller domain provides sites for attachment to other A-C linker components. The twist of A-C linker results in an iris diaphragm-like motion of the triplets in the longitudinal direction of procentriole. Finally, we identified two assembly intermediates at the growing ends of procentriole allowing us to propose a model for the procentriole assembly. Our results provide a comprehensive structural framework for understanding the molecular mechanisms underpinning procentriole biogenesis and assembly.

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Li, S., Fernandez, J.-J., Marshall, W., Agard, D.. 2018-10-12. Electron Cryo-Tomography Provides Insight into Procentriole Architecture and Assembly Mechanism. https://doi.org/10.1101/442590

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