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Nat Commun. 2018 Jul 13;9(1):2702. doi: 10.1038/s41467-018-05093-9.

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

Author information

1
Centre for Chromosome Biology, Biomedical Sciences, National University of Ireland Galway, Galway, Ireland, H91TK33.
2
Graduate Entry Medical School and Health Research Institute, University of Limerick, Limerick, V94 T9PX, Ireland.
3
Queen's University, Belfast, BT7 1NN, Northern Ireland, UK.
4
Centre for Chromosome Biology, Biomedical Sciences, National University of Ireland Galway, Galway, Ireland, H91TK33. elaine.dunleavy@nuigalway.ie.

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.

PMID:
30006572
PMCID:
PMC6045659
DOI:
10.1038/s41467-018-05093-9
[Indexed for MEDLINE]
Free PMC Article

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