大肠杆菌UvrC蛋白C端结构域的溶液结构及DNA结合特性
Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli.
作者信息
Singh S, Folkers G E, Bonvin A M J J, Boelens R, Wechselberger R, Niztayev A, Kaptein R
机构信息
Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
出版信息
EMBO J. 2002 Nov 15;21(22):6257-66. doi: 10.1093/emboj/cdf627.
Abstract
The C-terminal domain of the UvrC protein (UvrC CTD) is essential for 5' incision in the prokaryotic nucleotide excision repair process. We have determined the three-dimensional structure of the UvrC CTD using heteronuclear NMR techniques. The structure shows two helix-hairpin-helix (HhH) motifs connected by a small connector helix. The UvrC CTD is shown to mediate structure-specific DNA binding. The domain binds to a single-stranded-double-stranded junction DNA, with a strong specificity towards looped duplex DNA that contains at least six unpaired bases per loop ("bubble DNA"). Using chemical shift perturbation experiments, the DNA-binding surface is mapped to the first hairpin region encompassing the conserved glycine-valine-glycine residues followed by lysine-arginine-arginine, a positively charged surface patch and the second hairpin region consisting of glycine-isoleucine-serine. A model for the protein-DNA complex is proposed that accounts for this specificity.
摘要
UvrC蛋白的C末端结构域（UvrC CTD）在原核生物核苷酸切除修复过程中对5'切口至关重要。我们使用异核核磁共振技术确定了UvrC CTD的三维结构。该结构显示出两个由小连接螺旋连接的螺旋-发夹-螺旋（HhH）基序。已证明UvrC CTD介导结构特异性DNA结合。该结构域与单链-双链连接DNA结合，对每个环至少含有六个未配对碱基的环状双链DNA（“气泡DNA”）具有很强的特异性。通过化学位移扰动实验，将DNA结合表面定位到包含保守甘氨酸-缬氨酸-甘氨酸残基，随后是赖氨酸-精氨酸-精氨酸的第一个发夹区域，一个带正电荷的表面区域以及由甘氨酸-异亮氨酸-丝氨酸组成的第二个发夹区域。提出了一个蛋白质-DNA复合物模型来解释这种特异性。
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