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Centrioles are microtubule-based organelles crucial for cell division, sensing and motility. In Caenorhabditis elegans, the onset of centriole formation requires notably the proteins SAS-5 and SAS-6, which have functional equivalents across eukaryotic evolution. Whereas the molecular architecture of SAS-6 and its role in initiating centriole formation are well understood, the mechanisms by which SAS-5 and its relatives function is unclear. Here, we combine biophysical and structural analysis to uncover the architecture of SAS-5 and examine its functional implications in vivo. Our work reveals that two distinct self-associating domains are necessary to form higher-order oligomers of SAS-5: a trimeric coiled coil and a novel globular dimeric Implico domain. Disruption of either domain leads to centriole duplication failure in worm embryos, indicating that large SAS-5 assemblies are necessary for function in vivo.

Original publication

DOI

10.7554/eLife.07410

Type

Journal article

Journal

Elife

Publication Date

29/05/2015

Volume

4

Keywords

C. elegans, biophysics, cell biology, centrioles, crystallography, structural biology, structures, Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cell Cycle Proteins, Cell Division, Centrioles, Crystallography, X-Ray, DNA Mutational Analysis, Models, Molecular, Protein Conformation, Protein Multimerization, Protein Structure, Tertiary