The structure of T-aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases
The structure of T-aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases
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DOI：
10.1016/j.cell.2006.07.027
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发表时间：
2006-09-08
期刊：
影响因子：
64.5
通讯作者：
Steitz, Thomas A.
中科院分区：
文献类型：
--
作者：
Bailey, Scott;Wing, Richard A.;Steitz, Thomas A.
水生栖热菌DNA聚合酶III α亚基的晶体结构揭示了真细菌复制型聚合酶的催化结构域的结构与真核生物复制型聚合酶的催化结构域的结构无关，而是属于Pol β样核苷酸转移酶超家族。构建了与DNA和β-滑动夹两者复合的聚合酶与重定向结合结构域和内部β结合位点相互作用的模型，其与现有的生物化学数据一致。在晶体内，两个C-末端结构域通过比许多二聚体界面更大的表面相互作用。因为复制聚合酶;真细菌和真核生物/古细菌的复制聚合酶是不同源的，在最后的共同祖先的复制聚合酶的性质是未知的。虽然已经提出了其他的可能性，但应该考虑核酶DNA聚合酶的可降解性。
The crystal structure of Thermus aquaticus DNA polymerase III alpha subunit reveals that the structure of the catalytic domain of the eubacterial replicative polymerase is unrelated to that of the eukaryotic replicative polymerase but rather belongs to the Pol beta-like nucleotidyltransferase superfamily. A model of the polymerase complexed with both DNA and beta-sliding clamp interacting with a reoriented binding domain and internal beta binding site was constructed that is consistent with existing biochemical data. Within the crystal, two C-terminal domains are interacting through a surface that is larger than many dimer interfaces. Since replicative polymerases; of eubacteria and eukaryotes/archaea are not homologous, the nature of the replicative polymerase in the last common ancestor is unknown. Although other possibilities have been proposed, the plausibility of a ribozyme DNA polymerase should be considered.