Recognition of AT-rich DNA binding sites by the MogR repressor.

Recognition of AT-rich DNA binding sites by the MogR repressor.
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DOI:
10.1016/j.str.2009.02.018
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发表时间:
2009-05-13
期刊:
Structure (London, England : 1993)
影响因子:
--
通讯作者:
Panne D
Panne D
中科院分区:
其他
文献类型:
--
作者:
Shen A;Higgins DE;Panne D

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胞内病原体单核细胞增生李斯特菌的MogR转录抑制因子识别鞭毛基因启动子中富含AT的结合位点,以在感染期间下调鞭毛基因表达。本文描述了与flaA启动子区域内的识别序列5′ ATTTTTTAAAAAAAT 3′结合的MogR的1.8nm分辨率晶体结构。我们的结构表明,MogR作为二聚体结合。每个半位点在大沟中通过螺旋-转角-螺旋基序识别,在小沟中通过对称性相关分子的环识别,从而产生“交叉”结合模式。这种通过小沟相互作用的过采样对于特异性很重要。MogR结合位点具有A束DNA的结构特征,并且远离二聚体弯曲约52°。该结构解释了MogR如何在富含AT的L.单核细胞增多症和解释进化保守的A-道序列元件内的启动子区的MogR调控的鞭毛基因。
The MogR transcriptional repressor of the intracellular pathogen Listeria monocytogenes recognizes AT-rich binding sites in promoters of flagellar genes to down-regulate flagellar gene expression during infection. We describe here the 1.8Å resolution crystal structure of MogR bound to the recognition sequence 5′ ATTTTTTAAAAAAAT 3′ present within the flaA promoter region. Our structure shows that MogR binds as a dimer. Each half-site is recognized in the major groove by a helix-turn-helix motif and in the minor groove by a loop from the symmetry related molecule, resulting in a ‘cross-over’ binding mode. This oversampling through minor groove interactions is important for specificity. The MogR binding site has structural features of A-tract DNA and is bent by ~52° away from the dimer. The structure explains how MogR achieves binding specificity in the AT-rich genome of L. monocytogenes and explains the evolutionary conservation of A-tract sequence elements within promoter regions of MogR-regulated flagellar genes.
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