English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance R-loop structures pose a threat to genomic integrity because their formation can lead to mutagenesis. Mutagenesis drives antibiotic resistance in bacteria and chemotherapy resistance in human cancers; therefore, it is important to understand how R-loops form. Using a combination of in vitro single-molecule experimentation and in vivo mutagenesis assays, we have shown how Mfd, a bacterial protein known for its role in DNA repair, can interact with RNA polymerase to form R-loops. This interaction generates a topological domain in DNA that is highly prone to R-loop formation. The observed mechanism relies on properties of Mfd that are shared by many other proteins, hinting that this is a potentially universal model for R-loop formation.

Cotranscriptional R-loop formation by Mfd involves topological partitioning of DNA