Journal
JOURNAL OF CELL BIOLOGY
Volume 205, Issue 4, Pages 511-524Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201401009
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Funding
- Swedish research council
- Center for Biomembrane Research at Stockholm University
- Carl Tryggers foundation
- Knut and Alice Wallenberg Foundation
- National Institutes of Health [GM101386]
- Wenner-Gren Foundation (Stockholm, Sweden)
- M. Hildenbeutel through a post-doctoral stipend
- E.L. Hegg's stay in Stockholm
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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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