The homo-oligomerisation of both Sas-6 and Ana2 is required for efficient centriole assembly in flies

Matthew A. Cottee, Nadine Muschalik, Steven Johnson, Joanna Leveson, Jordan W. Raff, Susan M. Lea

Research output: Contribution to journalArticleResearchpeer-review

30 Citations (Scopus)

Abstract

Sas-6 and Ana2/STIL proteins are required for centriole duplication and the homo-oligomerisation properties of Sas-6 help establish the nine-fold symmetry of the central cartwheel that initiates centriole assembly. Ana2/STIL proteins are poorly conserved, but they all contain a predicted Central Coiled- Coil Domain (CCCD). Here we show that the Drosophila Ana2 CCCD forms a tetramer, and we solve its structure to 0.8 Å, revealing that it adopts an unusual parallel-coil topology. We also solve the structure of the Drosophila Sas-6 N-terminal domain to 2.9 Å revealing that it forms higher-order oligomers through canonical interactions. Point mutations that perturb Sas-6 or Ana2 homo-oligomerisation in vitro strongly perturb centriole assembly in vivo. Thus, efficient centriole duplication in flies requires the homo oligomerisation of both Sas-6 and Ana2, and the Ana2 CCCD tetramer structure provides important information on how these proteins might cooperate to form a cartwheel structure.

Original languageEnglish
Article numbere07236
Number of pages25
JournaleLife
Volume4
DOIs
Publication statusPublished - 23 May 2015
Externally publishedYes

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