Disease relevance of COQ5

• COQ5p is 43% identical to the polypeptide predicted by the Escherichia coli open reading frame, o251 (1) [1].

High impact information on COQ5

• Similarly, gel filtration chromatography shows that Coq1p, Coq3p, Coq4p, Coq5p, and Coq6p elute in fractions higher than expected for their respective subunit molecular masses [2].
• These studies show that at least two functions can be attributed to Coq5p; first, it is required to catalyze the C-methyltransferase step in Q biosynthesis and second, it is involved in stabilizing the Coq3 and Coq4 polypeptides required for Q biosynthesis [3].
• Yeast Coq5 C-methyltransferase is required for stability of other polypeptides involved in coenzyme Q biosynthesis [3].
• In this study we demonstrate that Coq5p is peripherally associated with the inner mitochondrial membrane on the matrix side [3].
• While C-methyltransferase activity is detectable in mitochondria isolated from this mutant, the steady state level of Coq5p is dramatically decreased [3].

Biological context of COQ5

• These results suggest that the regulation of COQ5 gene expression by carbon source is multifactorial and involves the interaction of various transcription factors [4].
• The COQ5 nucleotide sequence predicts a polypeptide of 307 amino acids containing a mitochondrial targeting signal [1].
• The COQ5 gene encodes a yeast mitochondrial protein necessary for ubiquinone biosynthesis and the assembly of the respiratory chain [1].
• A gene fusion expressing a biotinylated form of Coq5p retains function, as assayed by the complementation of the coq5 mutant [5].
• A nuclear gene, designated COQ5 was isolated from a yeast genomic library based on its ability to restore growth of a representative coq5 mutant on media containing glycerol as the sole carbon source [5].

Associations of COQ5 with chemical compounds

• Experiments performed using COQ5 promoter deletion/reporter constructs demonstrate a specific response to oleic acid [6].

References