A facile method for reversibly linking a recombinant protein to DNA.
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.
Goodman
Russell P
RP
Department of Physics, Clarendon Laboratory, University of Oxford, Parks Road, Oxford OX13PU, UK.
Erben
Christoph M
CM
Malo
Jonathan
J
Ho
Wei M
WM
McKee
Mireya L
ML
Kapanidis
Achillefs N
AN
Turberfield
Andrew J
AJ
D004247:DNA / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry; D009532:Nickel / Q000737:chemistry; D009571:Nitrilotriacetic Acid / Q000737:chemistry; D020411:Oligonucleotide Array Sequence Analysis; D009841:Oligonucleotides / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry*
C471213:His-His-His-His-His-His; D009841:Oligonucleotides; D009842:Oligopeptides; D011994:Recombinant Proteins; D006639:Histidine; D009532:Nickel; D004247:DNA; D009571:Nitrilotriacetic Acid