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Assembly of the three small Tim proteins precedes docking to the mitochondrial carrier translocase.

The mitochondrial intermembrane space contains a family of small Tim proteins that function as essential chaperones for protein import. The soluble Tim9-Tim10 complex transfers hydrophobic precursor proteins through the aqueous intermembrane space to the carrier translocase of the inner membrane (TIM22 complex). Tim12, a peripheral membrane subunit of the TIM22 complex, is thought to recruit a portion of Tim9-Tim10 to the inner membrane. It is not known, however, how Tim12 is assembled. We have identified a new intermediate in the biogenesis pathway of Tim12. A soluble form of Tim12 first assembles with Tim9 and Tim10 to form a Tim12-core complex. Tim12-core then docks onto the membrane-integrated subunits of the TIM22 complex to form the holo-translocase. Thus, the function of Tim12 in linking soluble and membrane-integrated subunits of the import machinery involves a sequential assembly mechanism of the translocase through a soluble intermediate complex of the three essential small Tim proteins.

Pubmed ID: 18421298

Authors

  • Gebert N
  • Chacinska A
  • Wagner K
  • Guiard B
  • Koehler CM
  • Rehling P
  • Pfanner N
  • Wiedemann N

Journal

EMBO reports

Publication Data

June 2, 2008

Associated Grants

None

Mesh Terms

  • Membrane Proteins
  • Membrane Transport Proteins
  • Mitochondrial ADP, ATP Translocases
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Proteins
  • Multiprotein Complexes
  • Protein Precursors
  • Protein Subunits
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins