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

Schulz, C., & Rehling, P. (2014). Remodelling of the active presequence translocase drives motor-dependent mitochondrial protein translocation. Nature Communications, 5: 4349. doi:10.1038/ncomms5349.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0023-D139-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-3D93-A
Genre: Journal Article

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 Creators:
Schulz, C., Author
Rehling, P.1, Author              
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1Max Planck Fellow Peter Rehling, ou_1298545              

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 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.

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Language(s): eng - English
 Dates: 2014-07-10
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms5349
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Title: Nature Communications
Source Genre: Journal
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Pages: 9 Volume / Issue: 5 Sequence Number: 4349 Start / End Page: - Identifier: -