Rapid, DNA-induced interface swapping by DNA gyrase

DNA gyrase, a ubiquitous bacterial enzyme, is a type IIA topoisomerase formed by heterotetramerisation of 2 GyrA subunits and 2 GyrB subunits, to form the active complex. GyrA is usually found as a dimer in solution, whereas GyrB can exist as a monomer. DNA gyrase is able to loop DNA around the C-terminal domains (CTDs) of GyrA and pass one DNA duplex through a transient double-strand break (DSB) established in another duplex. This results in the conversion of a positive loop into a negative one, thereby introducing negative supercoiling into the bacterial genome, an activity essential for DNA replication and transcription. The strong protein interface in the GyrA dimer must be broken to allow passage of the transported DNA segment and it is generally assumed that the interface is usually stable and only opens when DNA is transported, to prevent the introduction of deleterious DSBs in the genome. In this paper we show that DNA gyrase can exchange its DNA-cleaving interfaces between two ..., , , # Rapid, DNA-induced interface swapping by DNA gyrase

[https://doi.org/10.5061/dryad.w6m905qwn](https://doi.org/10.5061/dryad.w6m905qwn)

This repository contain most of the raw data presented in the article.

Organization:

For each figure and figure supplement, a corresponding zipped folder is available for download. They each contain a labelled file(s) for each subsection of the figure. The files format are .tif for gel picture, this is the output format from the imaging instrument, without any correction applied. These files can be used for quantification by densitometry. For the FPLC trace the file format is .txt containing the tab-separated values of the FPLC output. For the SPR and Mass Photometry data a .csv file is provided.

Accompanying each figure and figure supplement is a pdf file showing the annotated uncropped pictures when appropriate. Please refer to the following key for access to specific data.

Figure_1_figure_supplement_1.zip: zipped folder containing the followin...