Tbf1 and Vid22 promote resection and non-homologous end joining of DNA double-strand break ends
Tbf1 and Vid22 promote resection and non-homologous end joining of DNA double-strand break ends
复制标题
DOI：
10.1038/emboj.2012.327
复制
发表时间：
2013-01-23
期刊：
影响因子：
11.4
通讯作者：
Longhese, Maria Pia
中科院分区：
文献类型：
--
作者：
Bonetti, Diego;Anbalagan, Savani;Longhese, Maria Pia
DNA双链断裂(DSB)的修复是维持基因组稳定的关键。酿酒酵母蛋白Tbf1具有Myb结构域，与哺乳动物的TRF1和TRF2相关，被认为是一种转录激活因子。在这里，我们证明了Tbf1及其相互作用蛋白Vid22是响应DSB的新的参与者。TBF1或VID22的失活会导致对DSB诱导剂的超敏反应，并与影响同源重组的突变显示出强烈的负相互作用。此外，Tbf1和Vid22被招募到HO诱导的DSB中，在那里它们促进DNA末端的切除和非同源末端连接的修复。最后，Tbf1或Vid22的失活会损害DSB周围的核小体驱逐，这表明这些蛋白质通过影响周围染色质的特性来促进断裂的有效修复。EMBO期刊(2013)32,275-289。DOI：10.1038/Intemj.2012.327；2012年12月7日在线发布
The repair of DNA double-strand breaks (DSBs) is crucial for maintaining genome stability. The Saccharomyces cerevisiae protein Tbf1, which is characterized by a Myb domain and is related to mammalian TRF1 and TRF2, has been proposed to act as a transcriptional activator. Here, we show that Tbf1 and its interacting protein Vid22 are new players in the response to DSBs. Inactivation of either TBF1 or VID22 causes hypersensitivity to DSB-inducing agents and shows strong negative interactions with mutations affecting homologous recombination. Furthermore, Tbf1 and Vid22 are recruited to an HO-induced DSB, where they promote both resection of DNA ends and repair by non-homologous end joining. Finally, inactivation of either Tbf1 or Vid22 impairs nucleosome eviction around the DSB, suggesting that these proteins promote efficient repair of the break by influencing chromatin identity in its surroundings. The EMBO Journal (2013) 32, 275-289. doi:10.1038/emboj.2012.327; Published online 7 December 2012