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首页> 外文期刊>Nucleic Acids Research >DNA compaction by the higher-order assembly of PRH/Hex homeodomain protein oligomers
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DNA compaction by the higher-order assembly of PRH/Hex homeodomain protein oligomers

机译：通过PRH / Hex同源结构域蛋白寡聚体的高阶组装进行DNA压缩

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摘要

Protein self-organization is essential for the establishment and maintenance of nuclear architecture and for the regulation of gene expression. We have shown previously that the Proline-Rich Homeodomain protein (PRH/Hex) self-assembles to form oligomeric complexes that bind to arrays of PRH binding sites with high affinity and specificity. We have also shown that many PRH target genes contain suitably spaced arrays of PRH sites that allow this protein to bind and regulate transcription. Here, we use analytical ultracentrifugation and electron microscopy to further characterize PRH oligomers. We use the same techniques to show that PRH oligomers bound to long DNA fragments self-associate to form highly ordered assemblies. Electron microscopy and linear dichroism reveal that PRH oligomers can form protein-DNA fibres and that PRH is able to compact DNA in the absence of other proteins. Finally, we show that DNA compaction is not sufficient for the repression of PRH target genes in cells. We conclude that DNA compaction is a consequence of the binding of large PRH oligomers to arrays of binding sites and that PRH is functionally and structurally related to the Lrp/AsnC family of proteins from bacteria and archaea, a group of proteins formerly thought to be without eukaryotic equivalents.
机译：蛋白质的自组织对于建立和维持核结构以及调节基因表达至关重要。以前我们已经表明，脯氨酸丰富的Homeodomain蛋白（PRH / Hex）自组装形成寡聚复合物，它们以高亲和力和特异性结合到PRH结合位点阵列。我们还显示，许多PRH靶基因均含有适当间隔的PRH位点阵列，可使该蛋白质结合并调节转录。在这里，我们使用分析超速离心和电子显微镜进一步表征PRH低聚物。我们使用相同的技术来显示绑定到长DNA片段的PRH寡聚体自缔合以形成高度有序的程序集。电子显微镜和线性二向色性表明，PRH低聚物可以形成蛋白质-DNA纤维，并且PRH能够在不存在其他蛋白质的情况下压实DNA。最后，我们表明DNA压缩不足以抑制细胞中PRH靶基因。我们得出结论，DNA紧缩是大型PRH寡聚体与结合位点阵列结合的结果，并且PRH与细菌和古细菌的Lrp / AsnC家族蛋白在功能和结构上相关，这是以前被认为没有的一组蛋白真核等价物。

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