Beatty L G, Sadowski P D
Department of Medical Genetics, University of Toronto, Ontario, Canada.
J Mol Biol. 1988 Nov 20;204(2):283-94. doi: 10.1016/0022-2836(88)90576-1.
The FLP recombinase interacts with its target sequence with the formation of three distinct DNA-protein complexes. The first complex leaves neither a DNase footprint nor is the DNA protected from methylation by dimethyl sulfate. We have found, however, that the FLP protein is bound predominantly to only one of the three 13 base-pair (bp) symmetry elements. This asymmetric loading of the FLP site seems to require the presence of an adjacent directly repeated 13 bp element. We speculate that this asymmetric filling of the target site may be accompanied by the unique order of cleavage and exchange of DNA strands.
FLP重组酶与它的靶序列相互作用，形成三种不同的DNA-蛋白质复合物。第一种复合物既不留下DNA酶足迹，也不能使DNA免受硫酸二甲酯的甲基化作用。然而，我们发现，FLP蛋白主要仅与三个13碱基对（bp）对称元件中的一个结合。FLP位点的这种不对称加载似乎需要相邻直接重复的13 bp元件的存在。我们推测，靶位点的这种不对称填充可能伴随着DNA链切割和交换的独特顺序。
