English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
There are no MPG-Authors in the publication available
External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

2476872.pdf
(Publisher version), 3MB

Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-E0CF-0
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.