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  • 1.
    Gruschke, Steffi
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Römpler, Katharina
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Hildenbeutel, Markus
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Kehrein, Kirsten
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Kuehl, Inge
    Bonnefoy, Nathalie
    Ott, Martin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    The Cbp3-Cbp6 complex coordinates cytochrome b synthesis with bc(1) complex assembly in yeast mitochondria2012In: Journal of Cell Biology, ISSN 0021-9525, E-ISSN 1540-8140, Vol. 199, no 1, p. 137-150Article in journal (Refereed)
    Abstract [en]

    Respiratory chain complexes in mitochondria are assembled from subunits derived from two genetic systems. For example, the bc1 complex consists of nine nuclear encoded subunits and the mitochondrially encoded subunit cytochrome b. We recently showed that the Cbp3-Cbp6 complex has a dual function for biogenesis of cytochrome b: it is both required for efficient synthesis of cytochrome b and for protection of the newly synthesized protein from proteolysis. Here, we report that Cbp3-Cbp6 also coordinates cytochrome b synthesis with bc1 complex assembly. We show that newly synthesized cytochrome b assembled through a series of four assembly intermediates. Blocking assembly at early and intermediate steps resulted in sequestration of Cbp3-Cbp6 in a cytochrome b-containing complex, thereby making Cbp3-Cbp6 unavailable for cytochrome b synthesis and thus reducing overall cytochrome b levels. This feedback loop regulates protein synthesis at the inner mitochondrial membrane by directly monitoring the efficiency of bc1 complex assembly.

  • 2.
    Hildenbeutel, Markus
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Hegg, Eric L.
    Gruschke, Steffi
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Meunier, Brigitte
    Ott, Martin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    The timing of heme incorporation into yeast cytochrome bManuscript (preprint) (Other academic)
    Abstract [en]

    During oxidative phosphorylation electrons are transferred from NADH and succinate to the final electron acceptor oxygen by the complexes of the respiratory chain. These complexes carry redox active prosthetic groups that allow the transfer of electrons. Cytochrome b of the bc1 complex is encoded in the mitochondrial genome and acquires two heme b cofactors during its biogenesis. In this work we aimed to understand the mechanism and timing of cytochrome b hemylation. We provide evidence that cytochrome b present in the first bc1 complex assembly intermediate that contains the assembly factors Cbp3-Cbp6 and Cbp4 carries heme. This demonstrates that heme acquisition occurs very early during cytochrome b biogenesis. Moreover, by analyzing cytochrome b mutants lacking either of the two heme moieties, we reveal an obligate order of heme insertion into cytochrome b and suggest an incorporation mode from the intermembrane space. We propose a model in which Cbp3-Cbp6 keeps cytochrome b in a conformation allowing heme acquisition. Upon heme insertion, cytochrome b most likely undergoes a conformational change that enables binding of Cbp4, a pre-requisite for further assembly. Cbp4 thus might exhibit a proofreading function in hemylation.

  • 3.
    Hildenbeutel, Markus
    et al.
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Hegg, Eric L.
    Stephan, Katharina
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Gruschke, Steffi
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Meunier, Brigitte
    Ott, Martin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Assembly factors monitor sequential hemylation of cytochrome b to regulate mitochondria! translation2014In: Journal of Cell Biology, ISSN 0021-9525, E-ISSN 1540-8140, Vol. 205, no 4, p. 511-524Article in journal (Refereed)
    Abstract [en]

    Mitochondrial respiratory chain complexes convert chemical energy into a membrane potential by connecting electron transport with charge separation. Electron transport relies on redox cofactors that occupy strategic positions in the complexes. How these redox cofactors are assembled into the complexes is not known. Cytochrome b, a central catalytic subunit of complex III, contains two henne bs. Here, we unravel the sequence of events in the mitochondrial inner membrane by which cytochrome b is hemylated. Heme incorporation occurs in a strict sequential process that involves interactions of the newly synthesized cytochrome b with assembly factors and structural complex III subunits. These interactions are functionally connected to cofactor acquisition that triggers the progression of cytochrome b through successive assembly intermediates. Failure to hemylate cytochrome b sequesters the Cbp3-Cbp6 complex in early assembly intermediates, thereby causing a reduction in cytochrome b synthesis via a feedback loop that senses hemylation of cytochrome b.

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