Transmembrane helices mediate the formation of a stable ternary complex of b(5)R, cyt b(5), and SCD1.
Transmembrane helices mediate the formation of a stable ternary complex of b(5)R, cyt b(5), and SCD1.
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DOI:
10.1038/s42003-022-03882-z
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发表时间:
2022-09-12
影响因子:
5.9
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中科院分区:
文献类型:
--
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Mammalian cytochrome b5 (cyt b5) and cytochrome b5 reductase (b5R) are electron carrier proteins for membrane-embedded oxidoreductases. Both b5R and cyt b5 have a cytosolic domain and a single transmembrane (TM) helix. The cytosolic domains of b5R and cyt b5 contain cofactors required for electron transfer, but it is not clear if the TM helix has function beyond being an anchor to the membrane. Here we show that b5R and cyt b5 form a stable binary complex, and so do cyt b5 and stearoyl-CoA desaturase-1 (SCD1). We also show that b5R, cyt b5 and SCD1 form a stable ternary complex. We demonstrate that the TM helices are required for the assembly of stable binary and ternary complexes where electron transfer rates are greatly enhanced. These results reveal a role of the TM helix in cyt b5 and b5R, and suggest that an electron transport chain composed of a stable ternary complex may be a general feature in membrane-embedded oxidoreductases that require cyt b5 and b5R. The transmembrane domains of mammalian cytochrome b5 (cyt b5), cyt b5 reductase (b5R), and stearoyl-CoA desaturase-1 (SCD1) form stable binary complexes between cyt b5/b5R or cyt b5/SCD1 and a ternary complex, which enhance electron transfer rates.
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影响因子:
64.8
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19
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Im W
影响因子:
3.9
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MEYER, TE;SHIRABE, K;TOLLIN, G
通讯作者:
TOLLIN, G
影响因子:
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作者:
Jerabek, Petr;Florian, Jan;Martinek, Vaclav
通讯作者:
Martinek, Vaclav