Abstract:
AIMS:To investigate if one hypothetical protein from Chlamydophila pneumoniae AR39 exerts UbiG-like function by complementary experiments. METHODS AND RESULTS:Proteins UbiG have a signature S-adenosylmethionine-binding motif compared with other methyltransferases. Probing with the conserved motif, one hypothetical protein from C. pneumoniae AR39 was proposed to be a UbiG-like protein. The protein encoding the gene was used to swap its counterpart in Escherichia coli, and its expression in resultant strain DYCG was confirmed by RT-PCR. Strain DYCG grew on succinate as a carbon source, and rescued ubiquinone content in vivo, while the ubiG deletion strain DYK did not. CONCLUSIONS:Results indicate that the putative protein from C. pneumoniae exerts a UbiG-like function involved in ubiquinone biosynthesis. SIGNIFICANCE AND IMPACT OF THE STUDY:Identification of the ubiG-like gene will facilitate research on ubiquinone biosynthesis and aerobic respiration in the genus Chlamydophila owing to the important function of ubiquinone in vivo.
journal_name
Lett Appl Microbioljournal_title
Letters in applied microbiologyauthors
Liu J,Zhang X,Liu Jdoi
10.1111/j.1472-765X.2007.02144.xsubject
Has Abstractpub_date
2007-07-01 00:00:00pages
47-54issue
1eissn
0266-8254issn
1472-765Xpii
LAM2144journal_volume
45pub_type
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