Abstract：
:Coenzyme Q (Q) is a redox active lipid that is an essential component of the electron transport chain. Here, we show that steady state levels of Coq3, Coq4, Coq6, Coq7 and Coq9 polypeptides in yeast mitochondria are dependent on the expression of each of the other COQ genes. Submitochondrial localization studies indicate Coq9p is a peripheral membrane protein on the matrix side of the mitochondrial inner membrane. To investigate whether Coq9p is a component of a complex of Q-biosynthetic proteins, the native molecular mass of Coq9p was determined by Blue Native-PAGE. Coq9p was found to co-migrate with Coq3p and Coq4p at a molecular mass of approximately 1 MDa. A direct physical interaction was shown by the immunoprecipitation of HA-tagged Coq9 polypeptide with Coq4p, Coq5p, Coq6p and Coq7p. These findings, together with other work identifying Coq3p and Coq4p interactions, identify at least six Coq polypeptides in a multi-subunit Q biosynthetic complex.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Hsieh EJ,Gin P,Gulmezian M,Tran UC,Saiki R,Marbois BN,Clarke CFdoi
10.1016/j.abb.2007.02.016subject
Has Abstractpub_date
2007-07-01 00:00:00pages
19-26issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(07)00090-2journal_volume
463pub_type
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journal_title：Archives of biochemistry and biophysics
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