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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Decondensing the protamine domain for transcription
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Decondensing the protamine domain for transcription

机译：解冻鱼精蛋白结构域以进行转录

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摘要

Potentiation is the transition from higher-order, transcriptionally silent chromatin to a less condensed state requisite to accommodating the molecular elements required for transcription. To examine the underlying mechanism of potentiation an ≈ 13.7-kb mouse protamine domain of increased nuclease sensitivity flanked by 5' and 3' nuclear matrix attachment regions was defined. The potentiated DNase Ⅰ-sensitive region is formed at the pachytene spermatocyte stage with the recruitment to the nuclear matrix of a large ≈ 9.6-kb region just upstream of the domain. Attachment is then specified in the transcribing round spermatid, recapitulating the organization of the human cluster. In comparison to other modifiers that have no effect, i.e., histone methylation, HP1, and SATB1, topoisomerase engages nuclear matrix binding as minor marks of histone acetylation appear. Reorganization is marked by specific sites of topoisomerase Ⅱ activity that are initially detected in leptotene-zygotene spermatocytes just preceding the formation of the DNase Ⅰ-sensitive domain. This has provided a likely model of the events initiating potentiation, i.e., the opening of a chromatin domain.
机译：增强作用是从高阶，转录沉默的染色质过渡到容纳转录所需的分子元件所需的较少凝聚状态的过渡。为了检查潜在的增强机制，定义了一个核酸酶敏感性增加的≈13.7-kb小鼠鱼精蛋白结构域，其侧翼为5'和3'核基质附着区域。增强型DNaseⅠ敏感区形成于粗线期的精母细胞阶段，在结构域的上游募集了一个大的≈9.6kb区域的核基质。然后在转录的一轮精子细胞中指定附着，从而概括了人类簇的组织。与没有作用的其他修饰剂（即组蛋白甲基化，HP1和SATB1）相比，拓扑异构酶会随着组蛋白乙酰化的次要迹象而与核基质结合。重组以拓扑异构酶Ⅱ活性的特定位点为标志，该位点在DNaseⅠ敏感域形成之前，最初在瘦素-合子精子细胞中被检测到。这提供了引发增强作用的事件的可能模型，即染色质结构域的开放。

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