Journal
JOURNAL OF CELL BIOLOGY
Volume 216, Issue 1, Pages 83-92Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201607066
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Funding
- Deutsche Forschungsgemeinschaft (DFG) [SFB860, SFB746, SFB1190/Z03]
- Molecular Biology PhD program at the International Max Planck Research School
- Molecular Biology PhD program at Gottingen Graduate School for Neurosciences and Molecular Biosciences DFG grant [GSC 226/1]
- Excellence Initiative of the German federal and state governments [EXC 294 BIOSS]
- Centre National de la Recherche Scientifique-Institut National de la Sante et de la Recherche Medicale ATIP-Avenir program
- Boehringer Ingelheim Fonds
- Max Planck Society
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Two driving forces energize precursor translocation across the inner mitochondrial membrane. Although the membrane potential (Ay) 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 Delta psi. However, a precursor's hypersensitivity to a reduction of the Delta psi 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 Delta psi-driven translocation steps energize precursor passage across the inner mitochondrial membrane. The Delta psi- and Paml 17-dependent import step identified in this study is positioned between the two known energy-dependent steps: Delta psi-driven presequence translocation and adenosine triphosphate driven import motor activity.
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