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由 CENP-A 募集到着丝粒的 ATP 合酶 F 亚基对于雄性减数分裂是必需的。

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

机构信息

Centre for Chromosome Biology, Biomedical Sciences, National University of Ireland Galway, Galway, Ireland, H91TK33.

Graduate Entry Medical School and Health Research Institute, University of Limerick, Limerick, V94 T9PX, Ireland.

出版信息

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

DOI:10.1038/s41467-018-05093-9
PMID:30006572
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6045659/
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.

摘要

组蛋白 H3 变体 CENP-A 具有表观遗传定义着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着着。在这里,我们报告了 CENP-A 与线粒体 ATP 合酶复合物亚基在雄性果蝇生殖细胞中的相互作用。此外,我们报告说,CENP-A 以及亚基 ATPsyn-α、-β样(ATPsyn-β 的一种睾丸特异性同源物)和 -γ 的敲低会破坏减数分裂前期 I 中的姐妹着丝粒着丝粒。我们发现这种破坏可能与降低的 ATP 水平无关。我们发现 ATPsyn-α 和 -β样定位到减数分裂着丝粒,并且这种定位依赖于 CENP-A 的存在。我们表明,ATPsyn-α 在体外与 CENP-A 的 N 端直接相互作用,并且其 N 端的截断会破坏前期 I 中的姐妹着丝粒着丝粒。我们提出,CENP-A 的 N 端募集 ATPsyn-α 和 -β样到着丝粒上,以促进姐妹着丝粒在核功能中的着丝粒,该功能与氧化磷酸化无关。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/e2e3d56d8649/41467_2018_5093_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/c37052dbcaad/41467_2018_5093_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/91b05ef0c589/41467_2018_5093_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/7332b77b7673/41467_2018_5093_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/aa88d2c8d92b/41467_2018_5093_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/e2e3d56d8649/41467_2018_5093_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/c37052dbcaad/41467_2018_5093_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/91b05ef0c589/41467_2018_5093_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/7332b77b7673/41467_2018_5093_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/aa88d2c8d92b/41467_2018_5093_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2482/6045659/e2e3d56d8649/41467_2018_5093_Fig5_HTML.jpg

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