ATP synthase F1 subunits recruited to centromeres by CENP-A are required for male meiosis

Caitríona M. Collins, Beatrice Malacrida, Colin Burke, Patrick A. Kiely and Elaine M. Dunleavy ()
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Caitríona M. Collins: National University of Ireland Galway
Beatrice Malacrida: University of Limerick
Colin Burke: National University of Ireland Galway
Patrick A. Kiely: University of Limerick
Elaine M. Dunleavy: National University of Ireland Galway

Nature Communications, 2018, vol. 9, issue 1, 1-11

Abstract: Abstract The histone H3 variant CENP-A epigenetically defines the centromere and is critical for chromosome segregation. Here we report an interaction between CENP-A and subunits of the mitochondrial ATP synthase complex in the germline of male Drosophila. Furthermore, we report that knockdown of CENP-A, as well as subunits ATPsyn-α, -βlike (a testis-specific paralogue of ATPsyn-β) and -γ disrupts sister centromere cohesion in meiotic prophase I. We find that this disruption is likely independent of reduced ATP levels. We identify that ATPsyn-α and -βlike localise to meiotic centromeres and that this localisation is dependent on the presence of CENP-A. We show that ATPsyn-α directly interacts with the N-terminus of CENP-A in vitro and that truncation of its N terminus perturbs sister centromere cohesion in prophase I. We propose that the CENP-A N-terminus recruits ATPsyn-α and -βlike to centromeres to promote sister centromere cohesion in a nuclear function that is independent of oxidative phosphorylation.

Date: 2018
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DOI: 10.1038/s41467-018-05093-9

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