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. 2020 Jul 3;3:344. doi: 10.1038/s42003-020-1071-5

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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. 1 — a The protein constructs used in this study. For each construct, the first and last amino acid residue positions are shown. The box marks the deleted regions from amino acids 370–429. P-rich: proline-rich domain, RS: arginine/serine-rich domain, CED: central domain, RIIIDa and RIIIDb: RNase III domains, dsRBD: dsRNA-binding domain, Rhed: RNA-binding heme domain, and CTT: C-terminal tail region. b SDS-PAGE to show the purified G478 protein. c Structure diagrams and ribonucleotide sequences of 10L10_UGU and 10L10_noUGU. d The EMSAs for G478. Various amounts of G478 (ranging from 0 to 10 μM) were mixed with 1 μM of either 10L10_UGU or 10L10_noUGU in a 10 μL reaction solution. The reaction mixture was run on a 4% native PAGE gel. e Quantification of the EMSA data shown in (d). The density of each RNA band was measured using Image Lab 6.0 (Bio-Rad), and the results were obtained from three independent experiments.