Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair
Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair
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DOI：
10.1038/sj.emboj.7600222
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发表时间：
2004-05-19
期刊：
影响因子：
11.4
通讯作者：
Suh, SW
中科院分区：
文献类型：
--
作者：
Lee, BI;Kim, KH;Suh, SW
RecR与RecF和RecO一起促进了原核生物同源重组DNA修复的RecF途径中RecA的加载。人类Rad52蛋白是RecFOR的功能对应物。我们在这里展示了耐辐射球菌（DR RecR）的RecR晶体结构。DR RecR单体具有双结构域结构：n端结构域具有螺旋-发夹-螺旋（HhH）基序，c端结构域具有Cys(4)锌指结构域、Toprim结构域和Walker B基序。四个这样的单体形成一个222对称的环形四聚体，中心孔直径为30-35埃。在晶体中，两个四聚体是连接的，这意味着RecR四聚体能够打开和关闭。我们还发现DR RecR可以与dsDNA和ssDNA结合，并且它的HhH基序对于DNA结合是必不可少的。
RecR, together with RecF and RecO, facilitates RecA loading in the RecF pathway of homologous recombinational DNA repair in procaryotes. The human Rad52 protein is a functional counterpart of RecFOR. We present here the crystal structure of RecR from Deinococcus radiodurans (DR RecR). A monomer of DR RecR has a two-domain structure: the N-terminal domain with a helix-hairpin-helix (HhH) motif and the C-terminal domain with a Cys(4) zinc-finger motif, a Toprim domain and a Walker B motif. Four such monomers form a ring-shaped tetramer of 222 symmetry with a central hole of 30-35 Angstrom diameter. In the crystal, two tetramers are concatenated, implying that the RecR tetramer is capable of opening and closing. We also show that DR RecR binds to both dsDNA and ssDNA, and that its HhH motif is essential for DNA binding.