Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase η
Structure of the ubiquitin-binding zinc finger domain of human DNA Y-polymerase η
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DOI：
10.1038/sj.embor.7400901
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发表时间：
2007-03-01
期刊：
影响因子：
7.7
通讯作者：
Zhou, Pei
中科院分区：
文献类型：
--
作者：
Bomar, Martha G.;Pai, Ming-Tao;Zhou, Pei
人DNA Y家族聚合酶（pol）eta的泛素结合锌指（UBZ）结构域在跨损伤合成中聚合酶向停滞复制机制的募集中是重要的。在这里，我们报告的解决方案结构的pol eta UBZ结构域及其与泛素的相互作用。我们发现，UBZ域采用经典的C2 H2锌指结构，其特征在于由β-β-α倍。核磁共振滴定将UBZ和泛素之间的结合界面映射到UBZ结构域的α-螺旋和由残基L 8、144和V70限定的泛素的典型疏水表面。虽然UBZ结构域结合泛素通过一个单一的α-螺旋，在一种类似于倒泛素相互作用基序的方式，它的结构是不同于以前的特征泛素结合结构域。pol eta UBZ结构域代表C2 H2锌指家族的新成员，其与泛素相互作用以调节跨损伤合成。
The ubiquitin-binding zinc finger (UBZ) domain of human DNA Y-family polymerase (pol) eta is important in the recruitment of the polymerase to the stalled replication machinery in translesion synthesis. Here, we report the solution structure of the pol eta UBZ domain and its interaction with ubiquitin. We show that the UBZ domain adopts a classical C2H2 zinc-finger structure characterized by a beta beta alpha fold. Nuclear magnetic resonance titration maps the binding interfaces between UBZ and ubiquitin to the alpha-helix of the UBZ domain and the canonical hydrophobic surface of ubiquitin defined by residues L8, 144 and V70. Although the UBZ domain binds ubiquitin through a single alpha-helix, in a manner similar to the inverted ubiquitin-interacting motif, its structure is distinct from previously characterized ubiquitin-binding domains. The pol eta UBZ domain represents a novel member of the C2H2 zinc finger family that interacts with ubiquitin to regulate translesion synthesis.