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  1. Article

    Open Access

    Motor recruitment to the TIM23 channel’s lateral gate restricts polypeptide release into the inner membrane

    The presequence translocase of the mitochondrial inner membrane (TIM23 complex) facilitates anterograde precursor transport into the matrix and lateral release of precursors with stop-transfer signal into the ...

    Alexander Benjamin Schendzielorz, Piotr Bragoszewski… in Nature Communications (2018)

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  2. Article

    Open Access

    Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10

    The endoplasmic reticulum–mitochondria encounter structure (ERMES) connects the mitochondrial outer membrane with the ER. Multiple functions have been linked to ERMES, including maintenance of mitochondrial mo...

    Lars Ellenrieder, Łukasz Opaliński, Lars Becker, Vivien Krüger… in Nature Communications (2016)

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  3. No Access

    Article

    Motor-free mitochondrial presequence translocase drives membrane integration of preproteins

    The mitochondrial inner membrane is the central energy-converting membrane of eukaryotic cells. The electrochemical proton gradient generated by the respiratory chain drives the ATP synthase. To maintain this ...

    Martin van der Laan, Michael Meinecke, Jan Dudek, Dana P. Hutu… in Nature Cell Biology (2007)

  4. No Access

    Article

    Pam16 has an essential role in the mitochondrial protein import motor

    Mitochondrial preproteins destined for the matrix are translocated by two channel-forming transport machineries, the translocase of the outer membrane and the presequence translocase of the inner membrane. The...

    Ann E Frazier, Jan Dudek, Bernard Guiard… in Nature Structural & Molecular Biology (2004)

  5. Article

    Erratum: Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase

    Nature 401, 485— 489 (1999). In this paper, part of the labelling of Fig. 3 was printed incorrectly. The half-tones of Fig. 3a should have been labelled from left to right: Anti-Tom22 (lanes 1 and 2); Anti-Tom...

    Sandra van Wilpe, Michael T. Ryan, Kerstin Hill, Ammy C. Maarse, Chris Meisinger… in Nature (2000)

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  6. No Access

    Article

    Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase

    Mitochondrial preproteins are imported by a multisubunit translocase of the outer membrane (TOM), including receptor proteins and a general import pore1,2,3,4,5. The central receptor Tom22 binds preproteins throu...

    Sandra van Wilpe, Michael T. Ryan, Kerstin Hill, Ammy C. Maarse, Chris Meisinger… in Nature (1999)

  7. No Access

    Article

    Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22

    TRANSLOCATION of mitochondrial preproteins across the inner membrane is facilitated by the TIM machinery1–8. Tim23 binds to matrix targeting signals and initiates membrane potential-dependent import8. Tim23 and T...

    Christian Sirrenberg, Matthias F. Bauer, Bernard Guiard, Walter Neupert… in Nature (1996)

  8. No Access

    Article

    Mitochondrial Hsp70/MIM44 complex facilitates protein import

    Protein translocation into mitochondria requires the mitochondria! protein Hsp70. This molecular chaperone of the mitochondrial matrix is recruited to the protein import machinery by MIM44, a component associa...

    Hans-Christoph Schneider, Jutta Berthold, Matthias F. Bauer, Klaus Dietmeier… in Nature (1994)

  9. No Access

    Chapter

    Import of Cytochromes b2 and c1 into Mitochondria is Dependent on Both Membrane Potential and Nucleoside Triphosphates

    Import of precursors of cytochromes b2 and c1 into mitochondria requires a mitochondrial membrane potential. We show here that in addition ΔΨ, nucleoside triphosphates (NTPs) are necessary for protein translocati...

    Franz-Ulrich Hartl, Joachim Ostermann, Nikolaus Pfanner… in Cytochrome Systems (1987)

  10. No Access

    Chapter

    Two Different Species of Cytochrome b 5 in One Cell

    Cytochrome b 5 is traditionnaly extracted from liver microsomes. It is however known to be present in a number of other cell membrane fractions: nuclear membrane, Golgi membrane, plasma membrane, ...

    Florence Lederer, Rachid Ghrir, Bernard Guiard… in Methods in Protein Sequence Analysis (1982)

  11. No Access

    Article

    More similarity between bakers' yeast L-(+)-lactate dehydrogenase and liver microsomal cytochrome b5

    BAKERS' yeast L-lactate dehydrogenase, or cytochrome b2 (EC 1.1.2.3.), catalyses the oxidation of L-(+)-lactate to pyruvate. When purified in the presence of phenylmethane-sulphonylfluoride, it is a tetramer of f...

    BERNARD GUIARD, FLORENCE LEDERER, C. JACQ in Nature (1975)