Sharma, R, Davies, AG orcid.org/0000-0002-1987-4846 and Walti, C orcid.org/0000-0001-9286-5359 (2014) Directed Assembly of 3-nm-long RecA Nucleoprotein Filaments on Double-Stranded DNA with Nanometer Resolution. ACS Nano, 8 (4). pp. 3322-3330. ISSN 1936-0851
Abstract
Protein-mediated self-assembly is arguably one of the most promising routes for building complex molecular nanostructures. Here, we report a molecular self-assembly technique that allows programmable, site-specific patterning of double-stranded DNA scaffolds, at a single-base resolution, by 3-nm-long RecA-based nucleoprotein filaments. RecA proteins bind to single-stranded DNA to form nucleoprotein filaments. These can self-assemble onto a double-stranded DNA scaffold at a region homologous to the nucleoprotein’s single-stranded DNA sequence. We demonstrate that nucleoprotein filaments can be formed from single-stranded DNA molecules ranging in length from 60 nucleotides down to just 6 nucleotides, and these can be assembled site-specifically onto a model DNA scaffold both at the end of the scaffold and away from the end. In both cases, successful site-specific self-assembly is demonstrated even for the smallest nucleoprotein filaments, which are just 3 nm long, comprise only two monomers of RecA, and cover less than one helical turn of the double-stranded DNA scaffold. Finally, we demonstrate that the RecA-mediated assembly process is highly site-specific and that the filaments indeed bind only to the homologous region of the DNA scaffold, leaving the neighboring scaffold exposed.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2014, ACS. Reproduced in accordance with the publisher's self-archiving policy. This ACS article is provided to You under the terms of this ACS AuthorChoice/Editors’ Choice via Creative Commons CC-BY agreement. |
Keywords: | Self-assembly; nanomaterials; ReCa protein; triple-strand assembly; homologous recombination |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Electronic & Electrical Engineering (Leeds) > Pollard Institute (Leeds) The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 13 May 2014 12:15 |
Last Modified: | 20 Jun 2021 08:37 |
Published Version: | http://dx.doi.org/10.1021/nn405281s |
Status: | Published |
Publisher: | American Chemical Society |
Identification Number: | 10.1021/nn405281s |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:78726 |