STRUCTURAL ANALYSIS OF DNA REPAIR PROTEIN XRCC4 APPLYING CIRCULAR DICHROISM IN AN AQUEOUS SOLUTION.
STRUCTURAL ANALYSIS OF DNA REPAIR PROTEIN XRCC4 APPLYING CIRCULAR DICHROISM IN AN AQUEOUS SOLUTION.
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DOI：
10.1093/rpd/ncy275
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发表时间：
2019-05
影响因子：
1
通讯作者：
K. Nishikubo;Y. Izumi;Y. Matsumoto;K. Fujii;K. Matsuo;A. Yokoya
中科院分区：
文献类型：
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作者：
K. Nishikubo;Y. Izumi;Y. Matsumoto;K. Fujii;K. Matsuo;A. Yokoya
我们应用圆二色谱（CD）光谱分析，以获得DNA修复蛋白XRCC 4的二级结构，重点是其C-末端。使用同步辐射作为光源，在很宽的波长范围内，包括真空紫外（UV）光从180到200 nm和UV光从200到240 nm，我们确定了全长蛋白质的二级结构组成，包括其C-末端，这还没有-晶体学研究的重点，虽然它包含几个磷酸化位点。使用获得的CD光谱推断的二级结构表明，C-末端由大量的转角组成，具有少量无序和α-螺旋结构，几乎没有β-链。C末端可能形成以转角为主要成分的特征性二级结构，其DNA修复功能可能受末端磷酸化诱导的结构变化的调节。
We applied circular dichroism (CD) spectral analysis to obtain the secondary structure of the DNA repair protein XRCC4, with a focus on its C-terminus. Using synchrotron radiation as a light source across a wide range of wavelengths, including vacuum ultraviolet (UV) light from 180 to 200 nm and UV light from 200 to 240 nm, we determined the secondary structure composition of the full-length protein, including its C-terminus, which had not yet been -the focus of crystallography studies, though it contains several phosphorylation sites. The secondary structures inferred using the obtained CD spectra indicate that the C-terminus is composed of a substantial fraction of turns with a few unordered and alpha-helix structures and almost no beta-strands. The C-terminus is likely to form a characteristic secondary structure with turns as a main component, and its DNA repair function is likely regulated by the structural change induced by phosphorylation of the terminus.