Shu蛋白复合物在酵母细胞的DNA同源重组修复过程中行使重要功能，然而，在人的细胞中Shu蛋白复合物是如何组成以及Shu蛋白复合物的功能却并不清楚。在本研究论文中，黄俊教授课题组通过生化纯化方法克隆了一个新的蛋白SWSAP1/C19orf39，并发现SWSAP1能够与hSWS1组成人的细胞中的Shu蛋白复合物。实验发现该蛋白复合物具有单链DNA结合活性以及ATP酶活性，在细胞内降低SWSAP1的表达会减弱人的细胞的同源重组能力。这一研究结果表明Shu蛋白复合物在进化的过程中具有高度的保守性。华体会网址网页版,登录入口的刘婷博士和硕士研究生万力是这篇文章的共同第一作者。
hSWS1-SWSAP1 is an evolutionarily conserved complex required for efficient homologous recombination repair
Abstract
The Shu complex in yeast plays an important role in homologous recombination pathway, which is critical for the maintenance of genomic integrity. The identification of human SWS1 (hSWS1) as the homologue of budding yeast Shu2 implicated that the Shu complex is evolutionarily conserved. However, the human counterparts of other components in this complex have not yet been identified and characterized. Here we describe the characterization of a novel human component of this complex, SWSAP1 (hSWS1-associated protein 1) /C19orf39. We show that hSWS1 and SWSAP1 form a stable complex in vivo and in vitro. hSWS1 and SWSAP1 are mutually interdependent for their stability. We further demonstrate that the purified hSWS1-SWSAP1 complex possesses single-stranded DNA binding activity and DNA-stimulated ATPase activity. Moreover, SWSAP1 interacts with RAD51 and RAD51 paralogs and depletion of SWSAP1 causes defects in homologous recombination repair. Thus, our results suggest that the human Shu complex (hSWS1-SWSAP1) has an evolutionarily conserved function in homologous recombination.
原文链接：http://www.jbc.org/content/early/2011/09/28/jbc.M111.271080
