Goodman Russell P, Erben Christoph M, Malo Jonathan, Ho Wei M, McKee Mireya L, Kapanidis Achillefs N, Turberfield Andrew J
Department of Physics, Clarendon Laboratory, University of Oxford, Parks Road, Oxford OX13PU, UK.
Chembiochem. 2009 Jun 15;10(9):1551-7. doi: 10.1002/cbic.200900165.
We present a facile method for linking recombinant proteins to DNA. It is based on the nickel-mediated interaction between a hexahistidine tag (His(6)-tag) and DNA functionalized with three nitrilotriacetic acid (NTA) groups. The resulting DNA-protein linkage is site-specific. It can be broken quickly and controllably by the addition of a chelating agent that binds nickel. We have used this new linker to bind proteins to a variety of DNA motifs commonly used in the fabrication of nanostructures by DNA self-assembly.
我们提出了一种将重组蛋白与DNA连接的简便方法。它基于六组氨酸标签（His(6)-标签）与用三个次氮基三乙酸（NTA）基团功能化的DNA之间的镍介导相互作用。所得的DNA-蛋白质连接是位点特异性的。通过添加与镍结合的螯合剂，可以快速且可控地破坏这种连接。我们已使用这种新型连接子将蛋白质与DNA自组装制造纳米结构中常用的多种DNA基序结合。
