Meyer-Leon L, Huang L C, Umlauf S W, Cox M M, Inman R B
Department of Biochemistry, College of Agriculture and Life Sciences, University of Wisconsin-Madison 53706-1569.
Mol Cell Biol. 1988 Sep;8(9):3784-96. doi: 10.1128/mcb.8.9.3784-3796.1988.
Holliday structures are formed and resolved by FLP protein during site-specific recombination. These structures have been isolated and are visualized in both native and partially denatured states by electron microscopy. No single-strand breaks are found within the junction, indicating that the structure results from a reciprocal exchange of strands. These structures have properties consistent with being reaction intermediates. Double-strand cleavage products and "Y structures" are also detected and appear to be by-products of the reaction. The Y structures are three-armed branched molecules with a covalently closed junction located at the FLP recombination target site. Models are discussed, suggesting that both of these novel structures are made by aberrant cleavages during formation and resolution of the Holliday intermediate.
在位点特异性重组过程中，Holliday结构由FLP蛋白形成并解离。这些结构已被分离出来，并通过电子显微镜在天然状态和部分变性状态下可视化。在连接处未发现单链断裂，这表明该结构是由链的相互交换产生的。这些结构具有作为反应中间体的特性。还检测到双链切割产物和“Y结构”，它们似乎是该反应的副产物。Y结构是三臂分支分子，在FLP重组靶位点处有一个共价闭合的连接处。文中讨论了相关模型，表明这两种新结构都是在Holliday中间体形成和解离过程中异常切割产生的。
