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首页> 外文期刊>Journal of Molecular Biology >The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes.
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The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes.

机译：DNA促旋酶与细菌毒素CcdB的相互作用：存在两种促旋酶-CcdB复合物的证据。

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摘要

CcdB is a bacterial toxin that targets DNA gyrase. Analysis of the interaction of CcdB with gyrase reveals two distinct complexes. An initial complex (alpha) is formed by direct interaction between GyrA and CcdB; this complex can be detected by affinity column and gel-shift analysis, and has a proteolytic signature which is characterised by a 49 kDa fragment of GyrA. Surface plasmon resonance shows that CcdB binds to the N-terminal domain of GyrA with high affinity. In this mode of binding, CcdB does not affect the ability of gyrase to hydrolyse ATP or promote supercoiling. Incubation of this initial complex with ATP in the presence of GyrB and DNA slowly converts it to a second complex (beta), which has a lower rate of ATP hydrolysis and is unable to catalyse supercoiling. The efficiency of formation of this inactive complex is dependent on the concentrations of ATP and CcdB. We suggest that the conversion between the two complexes proceeds via an intermediate, whose formation is dependent on the rate of ATP hydrolysis. Copyright 1999 Academic Press.
机译：CcdB是一种靶向DNA促旋酶的细菌毒素。 CcdB与回旋酶相互作用的分析揭示了两个不同的复合物。初始复合物（alpha）是通过GyrA和CcdB之间的直接相互作用形成的;该复合物可通过亲和柱和凝胶位移分析检测，并具有蛋白水解特征，其特征在于49kDa的GyrA片段。表面等离子体共振表明，CcdB以高亲和力与GyrA的N末端域结合。在这种结合方式下，CcdB不会影响回旋酶水解ATP或促进超螺旋的能力。在GyrB和DNA的存在下，这种初始复合物与ATP一起孵育会缓慢地将其转化为第二种复合物（β），后者的ATP水解速率较低，并且无法催化超螺旋。这种无活性复合物的形成效率取决于ATP和CcdB的浓度。我们建议这两个复合物之间的转换是通过一个中间体进行的，该中间体的形成取决于ATP水解的速率。版权所有1999，学术出版社。

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