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. 2014 May 26;205(4):511–524. doi: 10.1083/jcb.201401009

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© 2014 Hildenbeutel et al.

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Figure 7. — Model for the stepwise hemylation of cytochrome b. Cytochrome b is synthesized by mitochondrial ribosomes that have the Cbp3–Cbp6 complex bound for efficient translation of the cytochrome b encoding mRNA. Newly synthesized cytochrome b interacts with Cbp3–Cbp6 in an unhemylated form in intermediate 0. Upon hemylation of the b_L site, the assembly factor Cbp4 is recruited to stabilize this heme incorporation. Hemylation of the b_H site provokes release of Cbp3–Cbp6 and the fully hemylated cytochrome b must interact with Qcr7 for stabilization. Cytochrome b in intermediate II is fully hemylated and ready for further assembly. Hemylation efficiency modulates synthesis of cytochrome b by a feedback loop involving Cbp3–Cbp6 sequestration in assembly intermediates 0 or I. When hemylation proceeds normally, Cbp3–Cbp6 is released for further stimulation of cytochrome b synthesis by mitochondrial ribosomes.