Atp synthase f1 subunits recruited to centromeres by cenp-a are required for male meiosis
Collins, Caitríona M. Malacrida, Beatrice Burke, Colin Kiely, Patrick A. Dunleavy, Elaine M.
Collins, Caitríona M.
Malacrida, Beatrice
Burke, Colin
Kiely, Patrick A.
Dunleavy, Elaine M.
Publication Date
2018-07-13
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Article
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Collins, Caitríona M. Malacrida, Beatrice; Burke, Colin; Kiely, Patrick A.; Dunleavy, Elaine M. (2018). Atp synthase f1 subunits recruited to centromeres by cenp-a are required for male meiosis. Nature Communications 9 ,
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-alpha, -beta like (a testis-specific paralogue of ATPsyn-beta) and -gamma disrupts sister centromere cohesion in meiotic prophase I. We find that this disruption is likely independent of reduced ATP levels. We identify that ATPsyn-alpha and -beta like localise to meiotic centromeres and that this localisation is dependent on the presence of CENP-A. We show that ATPsyn-alpha 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-alpha and -beta like to centromeres to promote sister centromere cohesion in a nuclear function that is independent of oxidative phosphorylation.
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Springer Nature
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Attribution-NonCommercial-NoDerivs 3.0 Ireland