Structural study of the function of Candida Albicans Pif1
Structural study of the function of Candida Albicans Pif1
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白色念珠菌Pif1功能的结构研究
DOI：
10.1016/j.bbrc.2021.06.050
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发表时间：
2021
影响因子：
3.1
通讯作者：
Xu-Guang Xi
中科院分区：
文献类型：
--
作者：
Ke-Yu Lu;Ben-Ge Xin;Teng Zhang;Na-Nv Liu;Dan Li;Stephane Rety;Xu-Guang Xi
Pif1解旋酶在真核生物中保守，在细胞核和线粒体中都参与维持基因组的稳定。在这里，我们报道了白色念珠菌Pif1(CaPif1368ATP883)与−及其类似物形成的复合体的晶体结构。我们的结果表明，Q基序负责识别腺嘌呤碱基，而CaPif1在dsDNA解离过程中优先利用ATP/dATP。虽然CaPif1与酿酒酵母Pif1在结构上有相似之处，但CaPif1可以通过氢键与DNA的胸苷碱基接触，而ScPif1不能。更重要的是，交联和突变实验表明，结构域2B的构象变化是CaPif1解开dsDNA所必需的。这些发现有助于进一步了解Pif1的解离机制。
Pif1 helicases, conserved in eukaryotes, are involved in maintaining genome stability in both the nucleus and mitochondria. Here, we report the crystal structure of a truncatedCandida AlbicansPif1 (CaPif1368−883) in complex with ssDNA and an ATP analog. Our results show that the Q-motif is responsible for identifying adenine bases, and CaPif1 preferentially utilizes ATP/dATP during dsDNA unwinding. Although CaPif1 shares structural similarities withSaccharomyces cerevisiaePif1, CaPif1 can contact the thymidine bases of DNA by hydrogen bonds, whereas ScPif1 cannot. More importantly, the crosslinking and mutant experiments have demonstrated that the conformational change of domain 2B is necessary for CaPif1 to unwind dsDNA. These findings contribute to further the understanding of the unwinding mechanism of Pif1.