Damage repair DNA polymerases Y.
Damage repair DNA polymerases Y.
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DOI：
10.1016/s0959-440x(02)00003-9
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发表时间：
2003-02
影响因子：
6.8
通讯作者：
Wei Yang
中科院分区：
文献类型：
--
作者：
Wei Yang
新发现的Y家族DNA聚合酶的特征在于使用未受损的模板进行低保真度复制和进行跨损伤DNA合成的能力。三个Y-家族聚合酶，单独或与DNA和核苷酸底物复合的晶体结构，揭示了一个传统的右手样催化核心组成的手指，拇指和手掌域。手指和拇指结构域非常小，导致开放和宽敞的活性位点，可以容纳错配的碱基对以及各种DNA损伤。Y家族聚合酶虽然没有3′→5′核酸外切酶活性，但具有独特的“小指”结构域，可促进DNA缔合、催化效率和与辅助因子的相互作用。Y-家族聚合酶的表达通常由DNA损伤诱导，并且它们向复制叉的募集在大肠杆菌中由β-clamp、clamp loader、单链DNA结合蛋白和RecA介导，在酵母中由泛素修饰的增殖细胞核抗原介导。
The newly found Y-family DNA polymerases are characterized by low fidelity replication using an undamaged template and the ability to carry out translesion DNA synthesis. The crystal structures of three Y-family polymerases, alone or complexed with DNA and nucleotide substrate, reveal a conventional right-hand-like catalytic core consisting of finger, thumb and palm domains. The finger and thumb domains are unusually small resulting in an open and spacious active site, which can accommodate mismatched base pairs as well as various DNA lesions. Although devoid of a 3′→5′ exonuclease activity, the Y-family polymerases possess a unique ‘little finger’ domain that facilitates DNA association, catalytic efficiency and interactions with auxiliary factors. Expression of Y-family polymerases is often induced by DNA damage, and their recruitment to the replication fork is mediated by β-clamp, clamp loader, single-strand-DNA-binding protein and RecA in Escherichia coli, and by ubiquitin-modified proliferating cell nuclear antigen in yeast.