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. 2019 Jul 24;9:10715. doi: 10.1038/s41598-019-47185-6

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© The Author(s) 2019

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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In vitro binding studies on RAN1, ETR1 and soluble copper chaperones by microscale thermophoresis (MST) (A) Dissociation constants of RAN1 and RAN1 truncation mutants with soluble copper chaperones ATX1, CCH and CCHΔ, respectively. (B) Dissociation constants of ETR1^1–157 and ETR1^306–738 with copper carriers RAN1, NterRAN1, CterRAN1, ATX1, CCH or CCHΔ, respectively. ETR1 interacts with both, the ATX-like chaperones and RAN1. Noteworthy, affinity of ETR1 for soluble copper chaperones is 10 fold lower than observed for ETR1 with full-length RAN1. For detailed binding curves see Fig. S3. (C) Copper transfer assay with purified recombinant Cu(I)-ATX1 or Cu(I)-CCH and ETR1^1–157. Copper content of ETR1^1–157 before (ETR1^1–157 only) and after (+ATX1, +CCH) incubation with preloaded donor copper chaperone. Increase in copper loading after chaperone incubation indicates chaperone mediated copper transfer to ETR1. Asterisks indicate significance level (p ≤ 0.001) determined using Student’s t-test.