Sluka J P, Horvath S J, Bruist M F, Simon M I, Dervan P B
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
Science. 1987 Nov 20;238(4830):1129-32. doi: 10.1126/science.3120311.
A synthetic 52-residue peptide based on the sequence-specific DNA-binding domain of Hin recombinase (139-190) has been equipped with ethylenediaminetetraacetic acid (EDTA) at the amino terminus. In the presence of Fe(II), this synthetic EDTA-peptide cleaves DNA at Hin recombination sites. The cleavage data reveal that the amino terminus of Hin(139-190) is bound in the minor groove of DNA near the symmetry axis of Hin recombination sites. This work demonstrates the construction of a hybrid peptide combining two functional domains: sequence-specific DNA binding and DNA cleavage.
一种基于Hin重组酶(139 - 190)序列特异性DNA结合结构域的52个残基的合成肽,在其氨基末端连接了乙二胺四乙酸(EDTA)。在Fe(II)存在的情况下,这种合成的EDTA肽在Hin重组位点切割DNA。切割数据表明,Hin(139 - 190)的氨基末端结合在Hin重组位点对称轴附近DNA的小沟中。这项工作展示了一种结合两个功能域的杂合肽的构建:序列特异性DNA结合和DNA切割。