title: Ubiquinone (coenzyme Q) biosynthesis in Chlamydophila pneumoniae AR39: identification of the ubiD gene.
abstract: Ubiquinone is an essential electron carrier in prokaryotes. Ubiquinone biosynthesis involves at least nine reactions in Escherichia coli. 3-octaprenyl-4-hydroxybenzoate decarboxylase (UbiD) is an important enzyme on the pathway and deletion of the ubiD gene in E. coli gives rise to ubiquinone deficiency in vivo. A protein from Chlamydophila pneumoniae AR39 had significant similarity compared with protein ubiD from E. coli. Based on this information, the protein-encoding gene was used to swap its counterpart in E. coli, and gene expression in resultant strain DYC was confirmed by RT-PCR. Strain DYC grew using succinate as carbon source and rescued ubiquinone content in vivo, while ubiD deletion strain DYD did not. Results suggest that the chlamydial protein exerts the function of UbiD.
authors.affiliation: College of Life Sciences & Technology, Shanghai Jiaotong University, Shanghai 200240, China.
authors.forename: Jun
authors.initials: J
authors.lastname: Liu
authors.forename: Jian-Hua
authors.initials: JH
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D002262:Carboxy-Lyases / Q000235:genetics* / Q000502:physiology; D016993:Chlamydophila pneumoniae / Q000201:enzymology* / Q000235:genetics*; D008969:Molecular Sequence Data; D014451:Ubiquinone / Q000096:biosynthesis*
chemical_list: D014451:Ubiquinone; C415986:3-octaprenyl-4-hydroxybenzoate carboxy-lyase; D002262:Carboxy-Lyases