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

Nature Communications
Caitríona M CollinsElaine M Dunleavy

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.

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Citations

Feb 8, 2020·Current Biology : CB·Nuria Cortes-SilvaInes A Drinnenberg
May 15, 2021·Life Science Alliance·Lisa E KurselHarmit S Malik

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Methods Mentioned

BETA
pull-down
PCR
RNA-Seq
Transgenic
peptide array

Software Mentioned

modENCODE
Image J
Prism
SoftWorx
StepOne

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ATP Synthases

ATP synthases are enzymes located in the inner mitochondrial membrane that catalyze the synthesis of ATP during cellular respiration. Discover the latest research on ATP synthases here.