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. 2023 Jan 23;25(3):467–480. doi: 10.1038/s41556-022-01074-9

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© The Author(s) 2023

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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Extended Data Fig. 10 — a, b, Wild type and mutant forms of EndoG (a) and SOD1 (b) were transfected in HeLa cells and analyzed for their mitochondrial import. Isolated mitochondria were resuspended in a hypotonic (osmotic swelling) buffer to generate mitoplasts. Proteinase K (10 μg/ml) was added to digest accessible proteins. Samples were analyzed by SDS-PAGE followed by immunoblotting using anti-GFP (EndoG or SOD1), anti-TOM20 (OM), anti-AIFM1 (IMS), anti-HCCS (IM), and anti-HSP60 (matrix) antibodies. Triton-X100 was added to solubilize matrix proteins and facilitate their proteinase K digestion, which revealed that mutant SOD1-G93A is partially protease-resistant as it is poorly digested even upon solubilization of all the different mitochondrial compartments. Results are representative of two replicates (a,b). Unprocessed blots are available in source data.

Source data