Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex.
Detailed mechanism for transposition by TnpA transposase involves DNA shape rather than direct protein-DNA recognition to generate an active nucleoprotein complex.
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DOI：
10.3410/b1-37
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发表时间：
2009-05-08
期刊：
影响因子：
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通讯作者：
Ho, P Shing
中科院分区：
文献类型：
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作者：
Ho, P Shing
Barabas及其同事确定的一系列单晶结构提供了幽门螺杆菌TnpA转座酶如何识别，切割和整合IS 200/IS 605类转座因子的详细机制。该机制的一个有趣方面是转座酶通过DNA组分序列所采用的独特折叠结构识别转座子，而不是通过直接的蛋白质-DNA相互作用。这是间接读出的一个例子，让人想起重组蛋白如何识别四链接头，但也类似于核糖核蛋白，因为DNA促进活性核酸-蛋白质复合物的形成。
A series of single-crystal structures determined by Barabas and colleagues provides a detailed mechanism for how the TnpA transposase from Helicobacter pylori recognizes, cleaves, and integrates the IS200/IS605 class of transposable elements. An interesting aspect of the mechanism is that the transposase recognizes the transposon through the unique fold-back structure adopted by the sequences of the DNA components, rather than through direct protein-DNA interactions. This is an example of indirect readout that is reminiscent of how four-stranded junctions are recognized by recombination proteins, but is also analogous to ribonucleoproteins, in that the DNA facilitates formation of an active nucleic acid-protein complex.