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. 2013 Apr 5;5(5):860–875. doi: 10.1093/gbe/evt056

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© The Author(s) 2013. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Fig. 3.— — Cellular localization of MPP subunits and core proteins in Trypanosoma brucei. (A) Immunoblot detection of MPP subunits and cp1 in cytosolic (Cyto) and mitochondrial (Mito) fractions isolated from T. brucei procyclic and bloodstream cells. The Rieske protein was used as a bc₁ complex marker. Cpn60, porin, and enolase were used as marker proteins of the mitochondrial matrix, mitochondrial membrane, and cytosol, respectively. (B) Immunoblot analysis of membrane and matrix fractions of T. brucei mitochondria isolated from procyclic trypanosomes. (C–F) Detection of α- and β-MPP subunits in transformed T. brucei. procyclic (C, D) and bloodstream (E, F) forms. The proteins were expressed with carboxy terminal hemagglutinin tag in procyclic cells (C, D) or V5 tag in bloodstream cells (E, F) and detected using mouse monoclonal anti-hemagglutinin and anti-V5 antibodies, respectively. Mitotracker was used as a control for the visualization of mitochondria.