论文部分内容阅读
Ubiquinone is an essential electron carrier in prokaryotes.Ubiquinone biosynthesis involves atleast nine reactions in Escherichia coli.3-octaprenyl-4-hydroxybenzoate decarboxylase (UbiD) is an importantenzyme 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 UbiDfrom E.coli.Based on this information,the protein-encoding gene was used to swap its counterpart inE.coli,and gene expression in resultant strain DYC was confirmed by RT-PCR.Strain DYC grew usingsuccinate 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.
Ubiquinone is an essential electron carrier in prokaryotes. Ubiquinone biosynthesis involves atleast nine reactions in Escherichia coli. 3-octaprenyl-4-hydroxybenzoate decarboxylase (UbiD) is an importanzyme 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. Strains 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.