The yeast Coq4 polypeptide organizes a mitochondrial protein complex essential for coenzyme Q biosynthesis.
The yeast Coq4 polypeptide organizes a mitochondrial protein complex essential for coenzyme Q biosynthesis.
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DOI:
10.1016/j.bbalip.2008.10.006
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发表时间:
2009-01
影响因子:
4.8
通讯作者:
Clarke, Catherine F.
中科院分区:
文献类型:
--
作者:
Marbois, Betn;Gin, Peter;Gulmezian, Melissa;Clarke, Catherine F.
Coenzyme Q is a redox active lipid essential for aerobic respiration. The Coq4 polypeptide is required for Q biosynthesis and growth on non-fermentable carbon sources, however its exact function in this pathway is not known. Here we probe the functional roles of Coq4p in a yeast Q biosynthetic polypeptide complex. A yeast coq4-1 mutant harboring an E226K substitution is unable to grow on nonfermentable carbon sources. The coq4-1 yeast mutant retains significant Coq3p O-methyltransferase activity, and mitochondria isolated from coq4-1 and coq4-2 (E121K) yeast point mutants contain normal steady state levels of Coq polypeptides, unlike the decreased levels of Coq polypeptides generally found in strains harboring coq gene deletions. Digitonin-solubilized mitochondrial extracts prepared from yeast coq4 point mutants show that Coq3p and Coq4 polypeptides no longer co-migrate as high molecular mass complexes by one- and two-dimensional Blue Native-PAGE. Similarly, gel filtration chromatography confirms that O-methyltransferase activity, Coq3p, Coq4p, and Coq7p migration are disorganized in the coq4-1 mutant mitochondria. The data suggest that Coq4p plays an essential role in organizing a Coq enzyme complex required for Q biosynthesis.
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影响因子:
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作者:
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通讯作者:
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DOI:
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