Respiratory chain supercomplexes associate with the cysteine desulfurase complex of the iron–sulfur cluster assembly machinery

Autor: Nicole Zufall, Jiyao Song, Nils Wiedemann, Lena Böttinger, Thomas Becker, Christoph U. Mårtensson
Rok vydání: 2018
Předmět:
Zdroj: Molecular Biology of the Cell
ISSN: 1059-1524
DOI: 10.1091/mbc.E17-09-0555
Popis: Mitochondrial cytochrome bc1 complex and cytochrome c oxidase associate in respiratory chain supercomplexes. We identified a specific association of the iron–sulfur cluster biogenesis desulfurase with the respiratory chain supercomplexes. Our finding reveals a novel link between respiration and iron–sulfur cluster formation.
Mitochondria are the powerhouses of eukaryotic cells. The activity of the respiratory chain complexes generates a proton gradient across the inner membrane, which is used by the F1FO-ATP synthase to produce ATP for cellular metabolism. In baker’s yeast, Saccharomyces cerevisiae, the cytochrome bc1 complex (complex III) and cytochrome c oxidase (complex IV) associate in respiratory chain supercomplexes. Iron–sulfur clusters (ISC) form reactive centers of respiratory chain complexes. The assembly of ISC occurs in the mitochondrial matrix and is essential for cell viability. The cysteine desulfurase Nfs1 provides sulfur for ISC assembly and forms with partner proteins the ISC-biogenesis desulfurase complex (ISD complex). Here, we report an unexpected interaction of the active ISD complex with the cytochrome bc1 complex and cytochrome c oxidase. The individual deletion of complex III or complex IV blocks the association of the ISD complex with respiratory chain components. We conclude that the ISD complex binds selectively to respiratory chain supercomplexes. We propose that this molecular link contributes to coordination of iron–sulfur cluster formation with respiratory activity.
Databáze: OpenAIRE