Two distinct membrane potential–dependent steps drive mitochondrial matrix protein translocation

2017 | journal article; research paper. A publication with affiliation to the University of Göttingen.

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​Two distinct membrane potential–dependent steps drive mitochondrial matrix protein translocation​
Schendzielorz, A. B. ; Schulz, C. ; Lytovchenko, O. ; Clancy, A. ; Guiard, B.; Ieva, R. & van der Laan, M. et al.​ (2017) 
The Journal of Cell Biology216(1) pp. 83​-92​.​ DOI: 

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Schendzielorz, Alexander Benjamin ; Schulz, Christian ; Lytovchenko, Oleksandr ; Clancy, Anne ; Guiard, Bernard; Ieva, Raffaele; van der Laan, Martin; Rehling, Peter 
wo driving forces energize precursor translocation across the inner mitochondrial membrane. Although the membrane potential (Δψ) is considered to drive translocation of positively charged presequences through the TIM23 complex (presequence translocase), the activity of the Hsp70-powered import motor is crucial for the translocation of the mature protein portion into the matrix. In this study, we show that mitochondrial matrix proteins display surprisingly different dependencies on the Δψ. However, a precursor's hypersensitivity to a reduction of the Δψ is not linked to the respective presequence, but rather to the mature portion of the polypeptide chain. The presequence translocase constituent Pam17 is specifically recruited by the receptor Tim50 to promote the transport of hypersensitive precursors into the matrix. Our analyses show that two distinct Δψ-driven translocation steps energize precursor passage across the inner mitochondrial membrane. The Δψ- and Pam17-dependent import step identified in this study is positioned between the two known energy-dependent steps: Δψ-driven presequence translocation and adenosine triphosphate-driven import motor activity.
Issue Date
The Journal of Cell Biology 
SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente 
SFB 1190 | Z03: Synthetische genetische Analyse, automatisierte Mikroskopie und Bildanalyse 
Working Group
RG Rehling (Mitochondrial Protein Biogenesis) 
RG Schwappach (Membrane Protein Biogenesis) 



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