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. 2017 May 9;8:15272. doi: 10.1038/ncomms15272

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Copyright © 2017, The Author(s)

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(a) Trypanosomal precursor proteins enter the mitochondrion through the ATOM translocase located in the outer membrane (OM). Tetracycline (Tet)-induced RNAi-mediated knockdown (+Tet) of the central protein import pore ATOM40 impairs import of precursor proteins into the organelle resulting in the depletion of mitochondrial proteins. (b) Immunoblots showing the steady-state levels of mitochondrial proteins in whole-cell extracts on Tet-induced RNAi of ATOM40. Proteins are: voltage-dependent anion channel (VDAC), cytochrome c (CYT C), cytochrome c oxidase subunit 4 (COXIV), cytochrome c1 (CYT C1), mitochondrial carrier protein 5 (MCP5), mitochondrial heat shock protein 70 (mtHSP70), and RNA-editing-associated protein 1 (REAP1). Precursors (p) and mature (m) protein forms are indicated. Cytosolic elongation factor 1 alpha (EF1α) serves as a control. Submitochondrial locations of proteins are indicated. IM, inner membrane; IMS, intermembrane space; OM, outer membrane. (c) Immunoblot analysis of whole cell (T) and digitonin-extracted, mitochondria-enriched pellet (P) and soluble (S) fractions of uninduced (−Tet) and induced (+Tet) ATOM40-RNAi cells. Precursor (p) and mature (m) protein forms are indicated. EF1a and VDAC serve as cytosolic and mitochondrial marker protein, respectively. (d) Northern blot analysis of mRNAs, isolated from uninduced (−Tet) and induced (+Tet) ATOM40-RNAi cells, coding for known mitochondrial proteins, which were strongly downregulated on ablation of ATOM40 (see Supplementary Data 1). Alpha-tubulin (α-TUB) serves as loading control. (e) Immunoblot analysis of mitochondrial proteins in whole-cell extracts from uninduced (−Tet) and induced (+Tet) ATOM40-RNAi cells cultured in the presence or absence of the proteasome inhibitor MG-132. Cytosolic EF1a serves as control.