Department of Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
Nature. 2012 Sep 27;489(7417):576-80. doi: 10.1038/nature11355. Epub 2012 Sep 9.
Chromosomal double-strand breaks (DSBs) are resected by 5' nucleases to form 3' single-stranded DNA substrates for binding by homologous recombination and DNA damage checkpoint proteins. Two redundant pathways of extensive resection have been described both in cells and in vitro, one relying on Exo1 exonuclease and the other on Sgs1 helicase and Dna2 nuclease. However, it remains unknown how resection proceeds within the context of chromatin, where histones and histone-bound proteins represent barriers for resection enzymes. Here we identify the yeast nucleosome-remodelling enzyme Fun30 as a factor promoting DSB end resection. Fun30 is the major nucleosome remodeller promoting extensive Exo1- and Sgs1-dependent resection of DSBs. The RSC and INO80 chromatin-remodelling complexes and Fun30 have redundant roles in resection adjacent to DSB ends. ATPase and helicase domains of Fun30, which are needed for nucleosome remodelling, are also required for resection. Fun30 is robustly recruited to DNA breaks and spreads along the DSB coincident with resection. Fun30 becomes less important for resection in the absence of the histone-bound Rad9 checkpoint adaptor protein known to block 5' strand processing and in the absence of either histone H3 K79 methylation or γ-H2A, which mediate recruitment of Rad9 (refs 9, 10). Together these data suggest that Fun30 helps to overcome the inhibitory effect of Rad9 on DNA resection.
染色体双链断裂(DSBs)被 5'核酸内切酶切除,形成 3'单链 DNA 底物,供同源重组和 DNA 损伤检查点蛋白结合。在细胞和体外都已经描述了两种广泛切除的冗余途径,一种依赖于 Exo1 核酸外切酶,另一种依赖于 Sgs1 解旋酶和 Dna2 核酸酶。然而,在染色质的背景下,组蛋白和组蛋白结合蛋白是切除酶的障碍,切除如何进行仍然未知。在这里,我们确定酵母核小体重塑酶 Fun30 是促进 DSB 末端切除的因素。Fun30 是主要的核小体重塑酶,可促进 DSB 处广泛的 Exo1 和 Sgs1 依赖性切除。RSC 和 INO80 染色质重塑复合物和 Fun30 在 DSB 末端附近的切除中具有冗余作用。需要用于核小体重塑的 Fun30 的 ATP 酶和解旋酶结构域也需要用于切除。Fun30 被强烈募集到 DNA 断裂处,并与切除同时沿着 DSB 扩散。在缺乏已知阻止 5'链加工的组蛋白结合 Rad9 检查点衔接蛋白的情况下,以及在缺乏介导 Rad9 募集的组蛋白 H3 K79 甲基化或 γ-H2A 的情况下,Fun30 对切除的重要性降低(参考文献 9、10)。这些数据表明,Fun30 有助于克服 Rad9 对 DNA 切除的抑制作用。