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Natural chromatin is heterogeneous and self-associates in vitro

机译:天然染色质在体外是异质的和自我联系

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The 30-nm fiber is commonly formed by oligonucleosome arrays in vitro but rarely found inside cells. To determine how chromatin higher-order structure is controlled, we used electron cryotomography (cryo-ET) to study the undigested natural chromatin released from two single-celled organisms in which 30-nm fibers have not been observed in vivo: picoplankton and yeast. In the presence of divalent cations, most of the chromatin from both organisms is condensed into a large mass in vitro. Rare irregular 30-nm fibers, some of which include face-to-face nucleosome interactions, do form at the periphery of this mass. In the absence of divalent cations, picoplankton chromatin decondenses into open zigzags. By contrast, yeast chromatin mostly remains condensed, with very few open motifs. Yeast chromatin packing is largely unchanged in the absence of linker histone and mildly decondensed when histones are more acetylated. Natural chromatin is therefore generally nonpermissive of regular motifs, even at the level of oligonucleosomes.
机译:30nm纤维通常通过体外寡核苷酸阵列形成,但很少在细胞内发现。为了确定如何控制染色蛋白的高阶结构,我们使用电子冷冻蛋白(Cryo-et)来研究从两种单细胞生物中释放的未消化的天然染色质,其中在体内尚未观察到30nm纤维:Picollankton和酵母。在二价阳离子的存在下,来自两种生物的大多数染色质在体外凝聚成大量质量。罕见的30nm纤维,其中一些包括面对面的核细胞体相互作用,在该质量周边形成形式。在没有二价阳离子的情况下,Picollankton染色质解体进入开放的曲折。相比之下,酵母染色质大多凝结,具有很少的开放式图案。在没有接头组蛋白的情况下,酵母染色质包装在很大程度上不变,当组蛋白更乙酰化时,在没有接头组蛋白和轻微的脱气的情况下。因此,即使在寡核苷的水平下,天然染色质通常也是常规基序的常规基序。

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