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

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  • Caitríona M. Collins

    (National University of Ireland Galway)

  • Beatrice Malacrida

    (University of Limerick)

  • Colin Burke

    (National University of Ireland Galway
    Queen’s University)

  • Patrick A. Kiely

    (University of Limerick)

  • Elaine M. Dunleavy

    (National University of Ireland Galway)

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.

Suggested Citation

  • Caitríona M. Collins & Beatrice Malacrida & Colin Burke & Patrick A. Kiely & Elaine M. Dunleavy, 2018. "ATP synthase F1 subunits recruited to centromeres by CENP-A are required for male meiosis," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05093-9
    DOI: 10.1038/s41467-018-05093-9
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