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. 2019 Jan 15;47(6):3142–3157. doi: 10.1093/nar/gky1308

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© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — The MLE dsRNA binding domains bind the first stem-loop of roX2–R2H1. (A) The domain organization of MLE helicase; the constructs used in this study are indicated. (B) Structural model of roX2 exon-3 showing the eight stem-loop structural domains linked together by flexible single-stranded linkers. The first stem-loop of roX2–R2H1 is highlighted with a dashed red box. (C) EMSAs with unlabeled 55mer R2H1 and identical increasing concentrations of MLE dsRBD constructs. (D) The binding affinities of 3′-FAM-labeled 55mer R2H1 for dsRBD₁ (red), dsRBD₂ (blue), dsRBD₁₊₂ (black) determined by FP experiments are shown.