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. 2019 Nov 25;10:1449. doi: 10.3389/fpls.2019.01449

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Copyright © 2019 Jain, Dashner and Connolly

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Mitochondrial localization of MIT proteins. Confocal images of onion peel epidermis transiently transformed with (A) 35S-MIT1-YFP and (B) 35S-MIT2-YFP constructs. The cells were co-stained with the mitochondria specific marker, MitoTracker Orange. (C) Mitochondria were purified from 2-week-old ArabidopsisMIT1-YFP-HA, MIT2-YFP-HA and the empty vector (EV-YFP-HA) transgenic lines grown on B5 media. 25 µg of the purified protein was separated by the SDS-PAGE. The localization of MIT1 and MIT2 was tested by immunoblotting with an anti-HA antibody. The chloroplast fraction (comprised of broken thylakoids/chloroplasts) separated from the mitochondrial fraction during ultracentrifugation were used as a control. The purity of the mitochondria was tested by immunoblotting the purified mitochondria against different cellular markers including COX2 and IDH (mitochondrial proteins), Actin (cytosolic protein), PSB-a (chloroplast protein) and Histone3 (nuclear protein). Ponceau S-stained proteins were used as a loading control. Note: the chloroplast MIT1-YFP-HA lane is overloaded relative to the MIT2-YFP-HA and EV-YFP-HA lanes.