1
Robert E. Jensen is in the Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
2
Arthur E. Johnson is in the Departments of Medical Biochemistry and Genetics, of Chemistry, and of Biochemistry and Biophysics, Texas A&M University Health Science Center, College Station, Texas 77843, USA.
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.
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