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. 2020 May 12;11:2355. doi: 10.1038/s41467-020-16146-3

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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. 4 — a Localization of Imp2-3xMyc was analyzed by density gradient centrifugation using purified organelles also containing the peroxisomal membrane protein Ant1 fused to YFP. Fraction were collected from the top of the gradient and analyzed by SDS–PAGE and western blot. Por1 is a protein located in the outer membrane of mitochondria. b Activity of Imp2-3xMyc was studied by analyzing the processing of the truncated Ptc5 variant Ptc5^1–201-RFP-HA. c Migration of Ptc5^1–201-RFP-PTS either containing (+MTS) or lacking (−MTS) the mitochondrial presequence was examined by SDS–PAGE and western blot. d The subcellular localization of ∆MTS Ptc5^1–201-RFP-PTS was investigated using fluorescence microscopy. White color indicates colocalization with the peroxisomal protein Ant1-YFP. Source data are provided in the Source data file.