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Unfolding of core nucleosomes by PARP-1 revealed by spFRET microscopy

机译：spFRET显微镜显示PARP-1核心核小体的展开

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DNA accessibility to various protein complexes is essential for various processes in the cell and is affected by nucleosome structure and dynamics. Protein factor PARP-1 (poly(ADP-ribose) polymerase 1) increases the accessibility of DNA in chromatin to repair proteins and transcriptional machinery, but the mechanism and extent of this chromatin reorganization are unknown. Here we report on the effects of PARP-1 on single nucleosomes revealed by spFRET (single-particle F?rster Resonance Energy Transfer) microscopy. PARP-1 binding to a double-strand break in the vicinity of a nucleosome results in a significant increase of the distance between the adjacent gyres of nucleosomal DNA. This partial uncoiling of the entire nucleosomal DNA occurs without apparent loss of histones and is reversed after poly(ADP)-ribosylation of PARP-1. Thus PARP-1-nucleosome interactions result in reversible, partial uncoiling of the entire nucleosomal DNA.
机译：DNA对各种蛋白质复合物的可及性对于细胞中的各种过程至关重要，并受核小体结构和动力学影响。蛋白质因子PARP-1（聚（ADP-核糖）聚合酶1）增加了染色质中DNA修复蛋白质和转录机制的可及性，但这种染色质重组的机制和程度尚不清楚。在这里，我们报告了spFRET（单粒子Fsterster共振能量转移）显微镜揭示的PARP-1对单核小体的影响。 PARP-1与核小体附近的双链断裂结合会导致核小体DNA相邻回旋之间的距离显着增加。整个核小体DNA的这种部分解开没有组蛋白的明显损失，并且在PARP-1的聚（ADP）-核糖基化之后被逆转。因此，PARP-1核小体相互作用导致整个核小体DNA发生可逆的部分解卷。

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