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. 2020 Mar 11;10:4481. doi: 10.1038/s41598-020-61432-1

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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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Purification and single-turnover kinetics of duplex RNA unwinding by the SCV helicase nsP13. (A) Lane 1, Protein marker, from bottom (in kilodaltons) 10, 20, 30, 40, 50 (strong density), 70, and 100. Lane 2, Crude cell extract without induction. Lane 3, Crude cell extract with IPTG induction. Lane 4, Proteins washed by nickel affinity chromatography. Lane 5, Helicase nsP13 eluted by nickel affinity chromatography. Lane 6, Helicase nsP13 eluted by size exclusion chromatography. (B) Schematic view of RNA duplex-unwinding by SCV helicase nsP13. (C) Representative native gel shift assay of RNA duplex unwinding by nsP13 with the 20U/15D RNA (5′-poly(U) tail of 20 bases/duplex length of 15 bp). The unwinding reaction was carried out at 37 °C for various times as described in the Materials and Methods section. The unwinding products were resolved by non-denaturing 15% PAGE. The gel was exposed to X-ray film and quantitated using image J software.