Abstract
After reconstitution into liposomes, Tim23p, a mitochondrial inner membrane protein required for protein import, forms an aqueous pore that is activated by a transmembrane potential and mitochondrial targeting peptides. A report in this issue suggests that proteins are translocated into the mitochondrial matrix through a channel formed by Tim23p. These data also suggest a mechanism by which protein import can occur without disrupting the permeablility barrier of the inner membrane.
Original language | English (US) |
---|---|
Pages (from-to) | 1008-1010 |
Number of pages | 3 |
Journal | Nature Structural Biology |
Volume | 8 |
Issue number | 12 |
DOIs | |
State | Published - 2001 |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics