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Identification of pathways for the uptake of Coenzyme Q in Saccharomyces cerevisiae
Author(s) -
Quinn Kelly,
James Andrew,
Murphy Michael,
Payne Gregory,
Clarke Catherine
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.715.44
Subject(s) - saccharomyces cerevisiae , complementation , biochemistry , mutant , yeast , biology , mitochondrial respiratory chain , coenzyme q – cytochrome c reductase , coenzyme q10 , mitochondrion , microbiology and biotechnology , gene , cytochrome c
Coenzyme Q (ubiquinone or Q) is an essential molecule required for aerobic respiration that helps transfer electrons and protons in the electron transport chain. Many eukaryotic cells, including the yeast Saccharomyces cerevisiae , are capable of de novo synthesis of Q. S. cerevisiae coq mutants lack the ability to synthesize Q, but respiration and growth on a nonfermentable carbon source is rescued when mutant yeast are supplied with exogenous Q containing 6 or 4 isoprenyl side chain groups in the tail (Q 6 or Q 4 ). Deletion of certain endocytosis genes prevents exogenous Q 6 from entering membranous organelles, including mitochondria (Padilla‐López et al. , Genetic evidence for the requirement of the endocytic pathway in the uptake of coenzyme Q 6 in Saccharomyces cerevisiae , 2009 BBA 1788, 1238). However, these same gene deletions do not affect rescue by less hydrophobic Q 4 (James et al. , Complementation of coenzyme Q‐deficient yeast by Q analogues requires the isoprenoid side chain, 2010 FEBS J 277, 2067). Here we examine selected yeast double mutants ( coq2Δ ORFΔ ) for the ability to grow on a nonfermentable carbon source in the presence of exogenously supplied Q 6 or Q 4 . These studies will identify genes and pathways required for trafficking of exogenously supplied Q to the mitochondria, potentially providing insights into mechanisms of Q 10 assimilation in humans. This research was supported by NSF MCB‐1330803.