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  Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import.

Denkert, N., Schendzielorz, A. B., Barbot, M., Versemann, L., Richter, F., Rehling, P., et al. (2017). Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import. eLife, 6: e28324. doi:10.7554/eLife.28324.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-E0CF-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-1DD2-2
Genre: Journal Article

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Denkert, N., Author
Schendzielorz, A. B., Author
Barbot, M., Author
Versemann, L., Author
Richter, F., Author
Rehling, P.1, Author              
Meinecke, M., Author
Affiliations:
1Max Planck Fellow Peter Rehling, ou_1298545              

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 Abstract: Virtually all mitochondrial matrix proteins and a considerable number of inner membrane proteins carry a positively charged, N-terminal presequence and are imported by the TIM23 complex (presequence translocase) located in the inner mitochondrial membrane. The voltage-regulated Tim23 channel constitutes the actual protein-import pore wide enough to allow the passage of polypeptides with a secondary structure. In this study, we identify amino acids important for the cation selectivity of Tim23. Structure based mutants show that selectivity is provided by highly conserved, pore-lining amino acids. Mutations of these amino acid residues lead to reduced selectivity properties, reduced protein import capacity and they render the Tim23 channel insensitive to substrates. We thus show that the cation selectivity of the Tim23 channel is a key feature for substrate recognition and efficient protein import.

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Language(s): eng - English
 Dates: 2017-08-31
 Publication Status: Published online
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.28324
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Title: eLife
Source Genre: Journal
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Pages: 16 Volume / Issue: 6 Sequence Number: e28324 Start / End Page: - Identifier: -