Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fluoride: insights into activator mechanochemical action
Binding of transcriptional activators to sigma 54 in the presence of the transition state analog ADP-aluminum fluoride: insights into activator mechanochemical action
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DOI：
10.1101/gad.205501
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发表时间：
2001-09-01
影响因子：
10.5
通讯作者：
Buck, M
中科院分区：
文献类型：
--
作者：
Chaney, M;Grande, R;Buck, M
西格玛54（西格玛（54））和西格玛（54）-全酶的构象变化取决于激活剂的核苷酸水解。我们现在证明，在 ADP-氟化铝（一种处于水解过渡态的 ATP 类似物）存在下，sigma (54) 及其全酶与转录激活剂 PspF 和 NifA 的中央 ATP 水解结构域结合。在 ADP-氟化铝存在的情况下，西格玛 (54) I 区与激活剂的直接结合已被证明，并从体内抑制遗传学推断出来。能量转导似乎是通过激活剂与 sigma (54) I 区接触而发生。ADP-氟化铝依赖性相互作用以及对其他 AAA+ 蛋白的考虑提供了对激活剂机械化学作用的深入了解。
Conformational changes in sigma 54 (sigma (54)) and sigma (54)-holoenzyme depend on nucleotide hydrolysis by an activator. We now show that sigma (54) and its holoenzyme bind to the central ATP-hydrolyzing domains of the transcriptional activators PspF and NifA in the presence of ADP-aluminum fluoride, an analog of ATP in the transition state for hydrolysis. Direct binding of sigma (54) Region I to activator in the presence of ADP-aluminum fluoride was shown and inferred from in vivo suppression genetics. Energy transduction appears to occur through activator contacts to sigma (54) Region I. ADP-aluminum fluoride-dependent interactions and consideration of other AAA+ proteins provide insight into activator mechanochemical action.