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. 2020 Mar 17;48(17):9762–9786. doi: 10.1093/nar/gkaa148

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© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Human YBEY is a bona fide mitochondrial protein. (A) The structural model (RaptorX) and the sequence of human YBEY. The predicted mitochondria-targeting peptide (TargetP) is highlighted in green. The diagnostic histidine triad of the UPF0054 family and the highly conserved R55 residue, mutated in this study, are shown in red. (B) Subcellular fractionation of HEK293T-REx cells supports a mitochondrial localization of endogenous YBEY. VDAC1 and HDAC2 are a mitochondrial and a nuclear marker, respectively. (C) Immunostaining of transiently transfected HepG2 cells expressing YBEY-FLAG. TOMM20 is used as mitochondrial marker. Scale bar, 10 μm. (D) Representative fluorescence intensity profiles of TOMM20 and YBEY-FLAG across a mitochondrion, derived from the experiment shown in (C), indicate the accumulation of YBEY in the interior space of mitochondria. (E) Submitochondrial localization of the YBEY-3 × FLAG protein. Crude mitochondria (‘Mito’), or mitochondria with the outer membrane ruptured by hypotonic swelling (‘Swelling’), or mitochondria lysed with 0.5% β-dodecyl maltoside (‘Lysed’) were treated (or not) with proteinase K and analysed by western blotting.