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首页> 外文期刊>Nucleic acids research >Nucleosome dynamics: HMGB1 relaxes canonical nucleosome structure to facilitate estrogen receptor binding
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Nucleosome dynamics: HMGB1 relaxes canonical nucleosome structure to facilitate estrogen receptor binding

机译：核小体动力学：HMGB1放松规范的核小体结构，促进雌激素受体结合

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High mobility group protein 1 (HMGB1) interacts with DNA and chromatin to influence the regulation of transcription, DNA repair and recombination. We show that HMGB1 alters the structure and stability of the canonical nucleosome (N) in a nonenzymatic, ATP-independent manner. Although estrogen receptor (ER) does not bind to its consensus estrogen response element within a nucleosome, HMGB1 restructures the nucleosome to facilitate strong ER binding. The isolated HMGB1-restructured nucleosomes (N′ and N″) remain stable and exhibit characteristics distinctly different from the canonical nucleosome. These findings complement previous studies that showed (i) HMGB1 stimulates in vivo transcriptional activation at estrogen response elements and (ii) knock down of HMGB1 expression by siRNA precipitously reduced transcriptional activation. The findings indicate that one aspect of the mechanism of HMGB1 action involves a restructuring of the nucleosome that appears to relax structural constraints within the nucleosome.
机译：高迁移率族蛋白1（HMGB1）与DNA和染色质相互作用，影响转录，DNA修复和重组的调控。我们显示HMGB1改变非酶，ATP独立方式的规范核小体（N）的结构和稳定性。尽管雌激素受体（ER）不会与核小体中的共识雌激素反应元件结合，但HMGB1会重组核小体以促进强ER结合。分离的HMGB1重组核小体（N'和N''）保持稳定，并表现出与典型核小体明显不同的特征。这些发现补充了先前的研究，这些研究表明（i）HMGB1刺激雌激素反应元件的体内转录激活，以及（ii）siRNA大大降低了转录激活，从而降低了HMGB1的表达。这些发现表明，HMGB1作用机制的一个方面涉及核小体的重组，这似乎放松了核小体内的结构限制。

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