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. 2017 Nov 1;8:1237. doi: 10.1038/s41467-017-01437-z

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© The Author(s) 2017

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. 5 — Atp10^ProtA accumulates with Atp6/Atp8-containing assembly intermediate in ina22Δ. a Chloramphenicol-pretreated wild type, Atp10^ProtA, and Atp10^ProtA ina22Δ mitochondria were subjected to in organello labeling for 20 min and IgG-affinity chromatography. Input and elution fractions were analyzed by SDS-PAGE (for Atp8 quantification) or urea SDS-PAGE (for Atp6 quantification), followed by digital autoradiography and western blotting (WB). Amounts of Atp6 and Atp8, isolated from Atp10^ProtA mitochondria, were set to 100%. Signals in the elution fraction were normalized to the amount of isolated Atp10^ProtA, (n = 3, ±SEM). b Chloramphenicol-pretreated wild type, Atp10^ProtA, and Atp10^ProtA ina22Δ mitochondria were subjected to in organello labeling for 20 min and IgG-affinity chromatography under low-stringency conditions and high-stringency conditions. Input and elution fractions were analyzed by SDS-PAGE, digital autoradiography, and western blotting (WB). Input = 1% of elution. c Chloramphenicol-pretreated wild type, Atp10^ProtA and Atp10^ProtA ina22Δ mitochondria were subjected to in organello labeling for 20 min and IgG-affinity chromatography. Complexes were eluted natively and elution fractions were analyzed by BN-PAGE and digital autoradiography. d Part of the elution fraction of the experiment presented in b, was analyzed by BN-PAGE, second dimension SDS-PAGE and digital autoradiography. e, f Chloramphenicol-pretreated wild type and ina22Δ mitochondria were subjected to in organello labeling for 15 min. Protein complexes were analyzed by BN-PAGE and second dimension urea SDS-PAGE (e) or SDS-PAGE (f) followed by digital autoradiography. Dashed boxes show Atp6/Atp8-containing assembly intermediates. g Chloramphenicol-pretreated wild type and ina22Δ mitochondria were analyzed by BN-PAGE, second dimension SDS-PAGE, and western blotting with the indicated antibodies. Dashed boxes show Atp23-containing complexes