IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v395y1998i6701d10.1038_26780.html
   My bibliography  Save this article

Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins

Author

Listed:
  • Kerstin Hill

    (Biophysik, Universität Osnabrück, FB Biologie/Chemie)

  • Kirstin Model

    (Institut für Biochemie und Molekularbiologie, Universität Freiburg)

  • Michael T. Ryan

    (Institut für Biochemie und Molekularbiologie, Universität Freiburg)

  • Klaus Dietmeier

    (Institut für Biochemie und Molekularbiologie, Universität Freiburg)

  • Falk Martin

    (Institut für Biochemie und Molekularbiologie, Universität Freiburg
    Fakultät für Biologie, Universität Freiburg)

  • Richard Wagner

    (Biophysik, Universität Osnabrück, FB Biologie/Chemie)

  • Nikolaus Pfanner

    (Institut für Biochemie und Molekularbiologie, Universität Freiburg)

Abstract

The mitochondrial outer membrane contains machinery for the import of preproteins encoded by nuclear genes1,2,3. Eight different Tom (translocase of outer membrane) proteins have been identified that function as receptors and/or are related to a hypothetical general import pore. Many mitochondrial membrane channel activities have been described4,5,6,7, including one related to Tim23 of the inner-membrane protein-import system5; however, the pore-forming subunit(s) of the Tom machinery have not been identified until now. Here we describe the expression and functional reconstitution of Tom40, an integral membrane protein with mainly β-sheet structure. Tom40 forms a cation-selective high-conductance channel that specifically binds to and transports mitochondrial-targeting sequences added to the cis side of the membrane. We conclude that Tom40 is the pore-forming subunit of the mitochondrial general import pore and that it constitutes a hydrophilic, ∼22 Å wide channel for the import of preproteins.

Suggested Citation

  • Kerstin Hill & Kirstin Model & Michael T. Ryan & Klaus Dietmeier & Falk Martin & Richard Wagner & Nikolaus Pfanner, 1998. "Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins," Nature, Nature, vol. 395(6701), pages 516-521, October.
    • Handle: RePEc:nat:nature:v:395:y:1998:i:6701:d:10.1038_26780
    DOI: 10.1038/26780
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/26780
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/26780?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Zhenzhen Chen & Qiankun He & Tiankun Lu & Jiayi Wu & Gaoli Shi & Luyun He & Hong Zong & Benyu Liu & Pingping Zhu, 2023. "mcPGK1-dependent mitochondrial import of PGK1 promotes metabolic reprogramming and self-renewal of liver TICs," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:395:y:1998:i:6701:d:10.1038_26780. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.