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Orthogonal Protein Assembly on DNA Nanostructures Using Relaxases

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

Otras publicaciones de la misma revista o congreso con autores/as de la Universidad de Cantabria

 Fuente: Angew Chem Int Ed Engl. 2016 Mar 18;55(13):4348-52

Editorial: Wiley

 Año de publicación: 2016

Nº de páginas: 5

Tipo de publicación: Artículo de Revista

DOI: 10.1002/anie.201510313

ISSN: 1521-3773,1433-7851

Autores/as

SAGREDO DE PEDRO, SANDRA

PIRZER, T.

AGHEBAT, RAFAT A

GOETZFRIED, MA