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. 2017 Mar 14;7:177. doi: 10.1038/s41598-017-00263-z

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© The Author(s) 2017

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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Mitochondrial localization of mitochondria-targeted DNA methyltransferases. (a) Confocal microscopy of HCT116 cells expressing MLS-mCherry-M.SssI. In order to stain the mitochondria, cells were incubated at 37 °C for 30 min. with 100 nM Mitotracker Deep Red. (b) Western blot of mitochondria-targeted M.CviPI, M.SssI or the catalytically inactive M.SssI ∆∆. Mitochondrial (MER) and nuclear (NER) protein extracts were isolated from C33A cells expressing mitochondria-targeted M.CviPI (lane 1) or M.SssI (lane 5) and HCT116 cells expressing mitochondria-targeted M.CviPI (lane 2), M.SssI (lane 3) or M.SssI ∆∆ (lane 4). A HAtag antibody was used to recognize the mitochondria-targeted constructs in the MER (49 kDa for M.CviPI, 52 kDa for M.SssI) or NER. Inside the mitochondria the mitochondrial-localization signal is cleaved off, reducing the size of the protein with 5 kDa. VDAC1/Porin (32 kDa) and Lamin B1 (68 kDa) were used as mitochondria and nuclear loading controls, respectively.

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