A mutation in the receiver domain of the Agrobacterium tumefaciens transcriptional regulator VirG increases its affinity for operator DNA.
A mutation in the receiver domain of the Agrobacterium tumefaciens transcriptional regulator VirG increases its affinity for operator DNA.
复制标题
根癌农杆菌转录调节因子 VirG 接收域的突变增加了其与操纵基因 DNA 的亲和力。
DOI：
10.1111/j.1365-2958.1994.tb00991.x
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发表时间：
1994
影响因子：
3.6
通讯作者：
Winans,SC
中科院分区：
文献类型：
--
作者：
Han,DC;Winans,SC
我们将野生型农杆菌和组成型virvirg54dallele与大肠杆菌的基因融合，并研究了MBP-VirG融合物与自调节virg启动子的结合。MBP-VirGN54D蛋白与该启动子结合的亲和力比MBP-VirG高10倍，与virbox I结合的亲和力比与virbox III结合的亲和力高8倍。virbox III的破坏并没有改变virbox I的亲和力，这表明这些位点之间缺乏协同性。我们提供的证据表明，与非结合蛋白相比，结合在单个virbox上的蛋白可能具有更高的低聚状态，并且在激活过程中可能发生邻近virbox I的DNA畸变。
We fused the wild‐typeAgrobacterium tumefaciens virGgene and the constitutivevirGN54Dallele to themalEgene ofEscherichia coli, and studied the binding of MBP—VirG fusions to the autoregulatedvirGpromoter. MBP—VirGN54D protein bound this promoter with 10‐fold higher affinity than MBP—VirG, and bound tovirbox I with eightfold higher affinity than tovirbox III. Disruption ofvirbox III did not alter the affinity forvirbox I, suggesting a lack of cooperativity between these sites. We provide evidence that protein bound at a singlevirbox may have a higher oligomeric state than non‐bound protein, and that a DNA distortion adjacent tovirbox I may occur during activation.