Assembly factors monitor sequential hemylation of cytochrome b to regulate mitochondrial translation.

Assembly factors monitor sequential hemylation of cytochrome b to regulate mitochondrial translation.
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DOI:
10.1083/jcb.201401009
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发表时间:
2014-05-26
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Ott M
Ott M
中科院分区:
其他
文献类型:
--
作者:
Hildenbeutel M;Hegg EL;Stephan K;Gruschke S;Meunier B;Ott M

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Assembly of the two heme b cofactors into the respiratory chain complex III subunit cytochrome b occurs in a step-by-step process that is monitored by assembly factors and regulates additional cytochrome b synthesis through a feedback loop. 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 heme 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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