Abstract：
:The biosynthesis of coenzyme Q presents a paradigm for how cells surmount hydrophobic barriers in lipid biology. In eukaryotes, CoQ precursors-among nature's most hydrophobic molecules-must somehow be presented to a series of enzymes peripherally associated with the mitochondrial inner membrane. Here, we reveal that this process relies on custom lipid-binding properties of COQ9. We show that COQ9 repurposes the bacterial TetR fold to bind aromatic isoprenes with high specificity, including CoQ intermediates that likely reside entirely within the bilayer. We reveal a process by which COQ9 associates with cardiolipin-rich membranes and warps the membrane surface to access this cargo. Finally, we identify a molecular interface between COQ9 and the hydroxylase COQ7, motivating a model whereby COQ9 presents intermediates directly to CoQ enzymes. Overall, our results provide a mechanism for how a lipid-binding protein might access, select, and deliver specific cargo from a membrane to promote biosynthesis.
journal_name
Mol Celljournal_title
Molecular cellauthors
Lohman DC,Aydin D,Von Bank HC,Smith RW,Linke V,Weisenhorn E,McDevitt MT,Hutchins P,Wilkerson EM,Wancewicz B,Russell J,Stefely MS,Beebe ET,Jochem A,Coon JJ,Bingman CA,Dal Peraro M,Pagliarini DJdoi
10.1016/j.molcel.2018.11.033subject
Has Abstractpub_date
2019-02-21 00:00:00pages
763-774.e10issue
4eissn
1097-2765issn
1097-4164pii
S1097-2765(18)31003-7journal_volume
73pub_type
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