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. 2019 Jan 21;20:1. doi: 10.1186/s12858-019-0104-5

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© The Author(s). 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 3 — Residue in H + 4 position alters ability of Ypd1 to function as a phosphorelay intermediate. Phosphoryl transfer reactions contained equimolar concentrations of Sln1-R1, Ypd1, and Ssk1-R2 proteins. Reactions were quenched at 5 min with stop buffer containing EDTA and separated by SDS-PAGE. The gel bands were detected by phosphorimaging and analyzed using ImageJ software. The amount of radiolabel in Ssk1-R2 bands in the presence of Ypd1-G68X mutants was quantified and compared with the amount of Ssk1-R2 radiolabel in the presence of wild-type Ypd1 (normalized to 100%)