kth.sePublications KTH
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
A DNA origami-based device for investigating DNA bending proteins by transmission electron microscopy
Department of Neuroscience and Biomedical Engineering, Aalto University, School of Science, P.O. Box 12200, FI-00076 Aalto, Finland .ORCID iD: 0000-0001-7897-708X
Department of Neuroscience and Biomedical Engineering, Aalto University, School of Science, P.O. Box 12200, FI-00076 Aalto, Finland .ORCID iD: 0000-0001-9894-5050
Department of Neuroscience and Biomedical Engineering, Aalto University, School of Science, P.O. Box 12200, FI-00076 Aalto, Finland .ORCID iD: 0000-0001-8060-6122
2023 (English)In: Nanoscale, ISSN 2040-3364, E-ISSN 2040-3372, Vol. 15, no 7, p. 3212-3218Article in journal (Refereed) Published
Abstract [en]

The DNA origami technique offers precise positioning of nanoscale objects with high accuracy. This has facilitated the development of DNA origami-based functional nanomechanical devices that enable the investigation of DNA-protein interactions at the single particle level. Herein, we used the DNA origami technique to fabricate a nanoscale device for studying DNA bending proteins. For a proof of concept, we used TATA-box binding protein (TBP) to evaluate our approach. Upon binding to the TATA box, TBP causes a bend to DNA of similar to 90 degrees. Our device translates this bending into an angular change that is readily observable with a conventional transmission electron microscope (TEM). Furthermore, we investigated the roles of transcription factor II A (TF(II)A) and transcription factor II B (TF(II)B). Our results indicate that TF(II)A introduces additional bending, whereas TF(II)B does not significantly alter the TBP-DNA structure. Our approach can be readily adopted to a wide range of DNA-bending proteins and will aid the development of DNA-origami-based devices tailored for the investigation of DNA-protein interactions.

Place, publisher, year, edition, pages
Royal Society of Chemistry (RSC) , 2023. Vol. 15, no 7, p. 3212-3218
National Category
Physical Chemistry
Identifiers
URN: urn:nbn:se:kth:diva-325191DOI: 10.1039/d2nr05366gISI: 000920185700001PubMedID: 36722916Scopus ID: 2-s2.0-85147339785OAI: oai:DiVA.org:kth-325191DiVA, id: diva2:1749694
Note

QC 20230411

Available from: 2023-04-11 Created: 2023-04-11 Last updated: 2024-08-27Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopus

Authority records

Ryssy, Joonas

Search in DiVA

By author/editor
Natarajan, Ashwin KarthickRyssy, JoonasKuzyk, Anton
In the same journal
Nanoscale
Physical Chemistry

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 98 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf