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dc.contributor.authorCollins, Caitríona M.
dc.contributor.authorMalacrida, Beatrice
dc.contributor.authorBurke, Colin
dc.contributor.authorKiely, Patrick A.
dc.contributor.authorDunleavy, Elaine M.
dc.identifier.citationCollins, 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 ,
dc.description.abstractThe 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.
dc.publisherSpringer Nature
dc.relation.ispartofNature Communications
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Ireland
dc.subjectsister-chromatid cohesion
dc.subjectshugoshin mei-s332
dc.titleAtp synthase f1 subunits recruited to centromeres by cenp-a are required for male meiosis

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