Abstract：
Human RAD52 protein binds DNA and is involved in genomic stability maintenance and several forms of DNA repair, including homologous recombination and single-strand annealing. Despite its importance, there are very few structural details about the variability of the RAD52 ring size and the RAD52 C-terminal protein-protein interaction domains. Even recent attempts to employ cryogenic electron microscopy (cryoEM) methods on full-length yeast and human RAD52 do not reveal interpretable structures for the C-terminal half that contains the replication protein A (RPA) and RAD51 binding domains. In this study, we employed the monodisperse purification of two RAD52 deletion constructs and small angle X-ray scattering (SAXS) to construct a structural model that includes RAD52\'s RPA binding domain. This model is of interest to DNA repair specialists as well as for drug development against HR-deficient cancers.
摘要：
人RAD52蛋白与DNA结合，参与基因组稳定性维持和几种形式的DNA修复，包括同源重组和单链退火。尽管它很重要,关于RAD52环大小和RAD52C端蛋白-蛋白相互作用域的变异性的结构细节很少。即使最近尝试在全长酵母和人RAD52上采用低温电子显微镜（cryoEM）方法，也没有揭示包含复制蛋白A（RPA）和RAD51结合域的C末端一半的可解释结构。在这项研究中,我们使用两个RAD52缺失构建体的单分散纯化和小角度X射线散射（SAXS）来构建包含RAD52的RPA结合域的结构模型。该模型对DNA修复专家以及针对HR缺陷癌症的药物开发感兴趣。
