Orthogonal Protein Assembly on DNA Nanostructures Using Relaxases
View/ Open
Full record
Show full item recordAuthor
Sagredo de Pedro, Sandra; Pirzer, T.; Aghebat, Rafat A; Goetzfried, MA; Moncalián Montes, Gabriel
Date
2016-03-18Derechos
Atribución-NoComercial-SinDerivadas 3.0 España
Publicado en
Angew Chem Int Ed Engl. 2016 Mar 18;55(13):4348-52
Publisher
Wiley
Abstract:
DNA-binding proteins are promising reagents for the sequence-specific modification of DNA-based nanostructures. Here, we investigate the utility of a series of relaxase proteins—TrwC, TraI, and MobA—for nanofunctionalization. Relaxases are involved in the conjugative transfer of plasmids between bacteria, and bind to their DNA target sites via a covalent phosphotyrosine linkage. We study the binding of the relaxases to two standard DNA origami structures—rodlike six-helix bundles and flat rectangular origami sheets. We find highly orthogonal binding of the proteins with binding yields of 40–50?% per binding site, which is comparable to other functionalization methods. The yields differ for the two origami structures and also depend on the position of the binding sites. Due to their specificity for a single-stranded DNA target, their orthogonality, and their binding properties, relaxases are a uniquely useful addition to the toolbox available for the modification of DNA nanostructures with proteins
Collections to which it belong
- D02 Artículos [306]