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A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6

Abstract:
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.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41598-019-40294-2

Authors

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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author


Publisher:
Springer Nature Publishing Group
Journal:
Scientific Reports More from this journal
Volume:
9
Article number:
3526
Publication date:
2019-03-05
Acceptance date:
2019-02-11
DOI:
ISSN:
2045-2322


Keywords:
Pubs id:
pubs:972278
UUID:
uuid:5e4af4e0-4138-4ca2-bbb1-f24c96b6786f
Local pid:
pubs:972278
Source identifiers:
972278
Deposit date:
2019-02-13
ARK identifier:

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