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A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6
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A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6
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A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6
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Journal Article
A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6
2019
Overview
Centrioles are conserved organelles fundamental for the organisation of microtubules in animal cells. Oligomerisation of the spindle assembly abnormal protein 6 (SAS-6) is an essential step in the centriole assembly process and may act as trigger for the formation of these organelles. SAS-6 oligomerisation is driven by two independent interfaces, comprising an extended coiled coil and a dimeric N-terminal globular domain. However, how SAS-6 oligomerisation is controlled remains unclear. Here, we show that in the
Caenorhabditis elegans
SAS-6, a segment of the N-terminal globular domain, unresolved in crystallographic structures, comprises a flexible loop that assists SAS-6 oligomerisation. Atomistic molecular dynamics simulations and nuclear magnetic resonance experiments suggest that transient interactions of this loop across the N-terminal dimerisation interface stabilise the SAS-6 oligomer. We discuss the possibilities presented by such flexible SAS-6 segments for the control of centriole formation.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82/16
/ Animals
/ Caenorhabditis elegans - metabolism
/ Caenorhabditis elegans Proteins - chemistry
/ Caenorhabditis elegans Proteins - genetics
/ Caenorhabditis elegans Proteins - metabolism
/ Cell Cycle Proteins - chemistry
/ Cell Cycle Proteins - genetics
/ Cell Cycle Proteins - metabolism
/ Humanities and Social Sciences
/ Humans
/ Molecular Dynamics Simulation
/ NMR
/ Nuclear Magnetic Resonance, Biomolecular
/ Recombinant Proteins - biosynthesis
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - isolation & purification
/ Science
/ Worms
