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. 2023 Mar 2;6:234. doi: 10.1038/s42003-023-04596-6

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© The Author(s) 2023

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. 7 — In the ES, PARP1 binds to and PARylates TRF1 decreasing its affinity for DNA duplex, that is functional for fork progression. In MS PARP1/TRF1 complexes are stabilized on single stranded DNA and recruit BLM and WRN that resolve secondary structures forming at the G-rich lagging strand. Created in BioRender.com.