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Opening the door to mitochondrial protein import

Nature Structural Biology volume 8, pages 1008–1010 (2001)Cite this article

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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Figure 1: Model of the mitochondrial protein import machinery.
Figure 2: Schematic diagram depicting the topography of Tim23p in the mitochondrial inner membrane.

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Authors and Affiliations

  1. the Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, 21205, Maryland, USA

    Robert E. Jensen

  2. 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

    Arthur E. Johnson

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  1. Robert E. Jensen
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  2. Arthur E. Johnson
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Correspondence to Robert E. Jensen or Arthur E. Johnson.

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Jensen, R., Johnson, A. Opening the door to mitochondrial protein import. Nat Struct Mol Biol 8, 1008–1010 (2001). https://doi.org/10.1038/nsb1201-1008

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