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Nuclear actin depolymerization in transcriptionally active avian and amphibian oocytes leads to collapse of intranuclear structures

机译:转录活性鸟类和两栖卵母细胞中的核肌动蛋白解聚导致核内结构崩溃

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Actin, which is normally depleted in the nuclei of somatic cells, accumulates in high amounts in giant nuclei of amphibian oocytes. The supramolecular organization and functions of this nuclear pool of actin in growing vertebrate oocyte are controversial. Here, we investigated the role of nuclear actin in the maintenance of the spatial architecture of intranuclear structures in avian and amphibian growing oocytes. A meshwork of filamentous actin was not detected in freshly isolated or fixed oocyte nuclei of Xenopus, chicken or quail. We found that the actin meshwork inside the oocyte nucleus could be induced by phalloidin treatment. Actin polymerization is demonstrated to be required to stabilize the specific spatial organization of nuclear structures in avian and amphibian growing oocytes. In experiments with the actin depolymerizing drugs cytochalasin D and latrunculin A, we showed that disassembly of nuclear actin polymers led to chromosome condensation and their transportation to a limited space within the oocyte nucleus. Experimentally induced “collapsing” of chromosomes and nuclear bodies, together with global inhibition of transcription, strongly resembled the process of karyosphere formation during oocyte growth.
机译:肌动蛋白通常被消耗在体细胞的核中,在两栖卵母细胞的巨核中大量积累。该肌动蛋白核池在正在生长的脊椎动物卵母细胞中的超分子组织和功能是有争议的。在这里,我们调查了核肌动蛋白在禽类和两栖类卵母细胞中维持核内结构空间结构的作用。在非洲爪蟾,鸡或鹌鹑的新鲜分离或固定的卵母细胞核中未检测到丝状肌动蛋白网。我们发现,鬼笔环肽处理可以诱导卵母细胞核内的肌动蛋白网状结构。已证明肌动蛋白聚合是稳定禽类和两栖类卵母细胞核结构特定空间组织所必需的。在肌动蛋白解聚药物细胞松弛素D和latrunculin A的实验中,我们表明核肌动蛋白多聚体的分解导致染色体凝结,并将其运输到卵母细胞核内的有限空间中。实验诱导的染色体和核体“塌陷”,以及转录的整体抑制,与卵母细胞生长过程中核球形成的过程非常相似。

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