Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China.
FEBS Lett. 2012 Jul 30;586(16):2306-12. doi: 10.1016/j.febslet.2012.06.024. Epub 2012 Jun 27.
In Saccharomyces cerevisiae, four proteins, Shu1, Shu2, Psy3 and Csm2, form a stable SHU-complex both in vivo and in vitro. These proteins are involved in the early stages of the homologous recombination DNA damage repair process. In this paper, the crystal structure of the Psy3-Csm2 sub-complex is presented at 1.8Å resolution and successfully fitted into our small angle X-ray scattering (SAXS) data of the SHU-complex. Taken together with our electrophoretic mobility shift assay (EMSA) results, a model is proposed for the SHU-protein complex coupled with DNA.
在酿酒酵母中, Shu1、Shu2、Psy3 和 Csm2 这四种蛋白质在体内和体外均形成稳定的 SHU 复合物。这些蛋白质参与同源重组 DNA 损伤修复过程的早期阶段。本文报道了 Psy3-Csm2 亚复合物的晶体结构,分辨率为 1.8Å,并成功拟合了我们的 SHU 复合物小角 X 射线散射(SAXS)数据。结合我们的电泳迁移率变动分析(EMSA)结果,提出了一个与 DNA 偶联的 SHU 蛋白复合物模型。