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. 2023 Feb 18;6:193. doi: 10.1038/s42003-023-04570-2

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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. 6 — a Ubl1 disrupts N-RNA binding in a dose-dependent manner according to EMSA assay. Lane C: ssRNA/ssDNA; Lane U: Ubl1 + ssRNA/ssDNA, Lane 0: N + ssRNA/ssDNA. Lanes 1–5, ssRNA/ssDNA plus different molar ratios of Ubl1 to N protein (from 1:5 to 5:5). The amount of free ssRNA/ssDNA from the N-RNA complex increases with increasing concentrations of Ubl1 in Lanes 1–5. b Curve fit of MST traces for determination of the N-ssRNA binding affinity. c–e The binding affinity of N protein and ssRNA decreases with the addition of 1 μM (c), 5 μM (d) and 10 μM (e) of Ubl1. No interaction between Ubl1 and ssRNA was detected (c–e, right). The error bar represents the standard error of the mean of three independent experiments (n = 3).