Unexpected structural diversity in DNA recombination: The restriction endonuclease connection
Unexpected structural diversity in DNA recombination: The restriction endonuclease connection
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DOI：
10.1016/s1097-2765(00)80267-1
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发表时间：
2000-06-01
期刊：
影响因子：
16
通讯作者：
Dyda, F
中科院分区：
文献类型：
--
作者：
Hickman, AB;Li, Y;Dyda, F
转座需要一系列协调的DNA断裂和连接反应。Tn7转座酶含有两种蛋白质：TnsA，在转座子的5'末端进行DNA断裂，和TnsB，在转座子的3'末端进行断裂和连接。TnsB是逆转录病毒整合酶超家族的成员，其标志是保守的DDE基序。我们在这里报告在2.4埃分辨率的TnsA结构。令人惊讶的是，TnsA折叠是II型限制性内切核酸酶的折叠。因此，Tn7转座涉及多肽之间的协作，一个含有DDE基序，一个不含。这一结果表明，利用限制酶样折叠的生物过程的范围也包括DNA转座。
Transposition requires a coordinated series of DNA breakage and joining reactions. The Tn7 transposase contains two proteins: TnsA, which carries out DNA breakage at the 5' ends of the transposon, and TnsB, which carries out breakage and joining at the 3' ends of the transposon. TnsB is a member of the retroviral integrase superfamily whose hallmark is a conserved DDE motif. We report here the structure of TnsA at 2.4 Angstrom resolution. Surprisingly, the TnsA fold is that of a type II restriction endonuclease. Thus, Tn7 transposition involves a collaboration between polypeptides, one containing a DDE motif and one that does not. This result indicates that the range of biological processes that utilize restriction enzyme-like folds also includes DNA transposition.