Remodelling of the active presequence translocase drives motor-dependent mitochondrial protein translocation

Christian Schulz and Peter Rehling ()
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Christian Schulz: University Medical Center Göttingen
Peter Rehling: University Medical Center Göttingen

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract Proteins with N-terminal targeting signals are transported across the inner mitochondrial membrane by the presequence translocase. To drive precursor translocation, the Hsp70-import motor associates with the protein-conducting channel of the TIM23 complex. It is unknown how the ATPase cycle of Hsp70 is regulated in the context of a translocating polypeptide chain. Here we establish an assay to monitor protein dynamics in the precursor-occupied presequence translocase and find that regulatory subunits of the import motor, such as the ATPase-stimulating J-protein Pam18, are recruited into the translocation intermediate. The presence of all Hsp70 co-chaperones at the import channel is not sufficient to promote matrix protein import, instead a recharging of the active translocase with Pam18 is required for motor activity. Thus, a replenishment cycle of co-chaperones at the TIM23 complex is an integral part of Hsp70’s ATPase cycle at the channel exit site and essential to maintain motor-driven mitochondrial protein import.

Date: 2014
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DOI: 10.1038/ncomms5349

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