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. 2020 Mar 20;11:1478. doi: 10.1038/s41467-020-15182-3

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — a In cells, Mfd is normally auto-inhibited and does not stably interact with DNA. Binding to stressed TECs via its RNAP interacting domain leads to release of inhibition and a large conformational change in the protein. Following this, the motor domain engages DNA on the upstream edge of the transcription bubble and subsequent ATP hydrolysis leads to either transcription reactivation/termination. Mfd continues to translocate on dsDNA after remodeling the RNAP. Meanwhile, the UvrB homology module of Mfd is exposed permitting recruitment of UvrA. ATP hydrolysis at UvrA’s distal ATPase site is necessary for this engagement. Engagement with UvrA₂ leads to arrest of translocation. Further, recruitment of UvrB (either sequentially as shown, or simultaneously with UvrA₂) to the site leads to formation of the Mfd-UvrA-UvrA-UvrB handoff complex. Subsequent ATP hydrolysis at UvrA’s proximal ATPase site results in loading of UvrB on the DNA. Successful engagement of UvrB with the DNA via its β-hairpin is necessary for completing the handoff, culminating in dissociation of Mfd and UvrA₂ from the site. b Facilitated dissociation model operates inside cells resulting in the simultaneous loss of UvrA₂ and Mfd from the site of transcriptional stress.