Cyclobutylpyrimidine dimer base flipping by DNA photolyase
Cyclobutylpyrimidine dimer base flipping by DNA photolyase
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DOI：
10.1074/jbc.m206531200
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发表时间：
2002-10-11
影响因子：
4.8
通讯作者：
Stanley, RJ
中科院分区：
文献类型：
--
作者：
Christine, KS;MacFarlane, AW;Stanley, RJ
DNA光裂合酶是一种黄素蛋白，利用光修复DNA中的环丁基嘧啶二聚体。从蛋白质的晶体结构的考虑，已经假设二聚体损伤从DNA双螺旋翻转到底物结合口袋中。我们已经使用了荧光腺嘌呤类似物，2-氨基嘌呤（2-Ap），作为探针的本地双螺旋结构后结合的底物的蛋白质。我们的研究结果表明，胸苷损伤周围的局部结构发生显着变化后，绑定到Photolyase。这与损伤进入蛋白结合腔的碱基翻转以及伴随的相对互补2-Ap核苷酸的去堆积一致。
DNA Photolyase is a flavoprotein that uses light to repair cyclobutylpyrimidine dimers in DNA. From considerations of the crystal structure of the protein, it has been hypothesized that the dimer lesion is flipped out of the DNA double helix into the substrate binding pocket. We have used a fluorescent adenine analog, 2-aminopurine (2-Ap), as a probe of local double helical structure upon binding of the substrate to the protein. Our results show that the local structure around the thymidine lesion changes dramatically upon binding to Photolyase. This is consistent with base flipping of the lesion into the protein binding cavity with concomitant destacking of the opposing complementary 2-Ap nucleotide.