![]() ![]() ![]() We further hypothesize that the observed mode of CYP153 gene regulation is shared by many Actinobacteria.īiodegradation of petroleum hydrocarbons is an important process for both natural oil attenuation and industrial applications, such as microbial enhanced oil recovery (MEOR) ( 1) and bioremediation of oil-contaminated environments ( 2, 3). ![]() By comparing CYP153 gene arrangements in Actinobacteria and Proteobacteria, we found that the AraC family regulator is ubiquitously located upstream of the CYP153 gene, suggesting its universal regulatory role in CYP153 gene transcription. Moreover, we constructed a cypR mutant strain and found that the CYP153 gene promoter activities and CYP153 gene transcriptional levels in the mutant strain were depressed compared with those in the wild-type strain in the presence of n-alkanes, suggesting that CypR served as an activator for the CYP153 gene promoter. Further analysis of the β-galactosidase activity in the CYP153 gene promoter- lacZ fusion cell indicated that the CYP153 gene promoter was induced by n-alkanes comprised of 8 to 14 carbon atoms, but not by derived decanol and decanic acid. Sequence alignment of upstream regions of CYP153 gene clusters revealed high conservation in the −10 and −35 regions in Actinobacteria. We first identified the transcriptional start site and the promoter of the CYP153 gene cluster. In this paper, we studied CYP153 gene transcription regulation by the potential AraC family regulator (CypR) located upstream of the CYP153 gene cluster in a broad-spectrum n-alkane-degrading Gram-positive bacterium, Dietzia sp. However, the mechanisms regulating the expression of the protein remain largely unknown. CYP153 is also thought to cooperate with AlkB in degrading various n-alkanes. CYP153, one of the most common medium-chain n-alkane hydroxylases belonging to the cytochrome P450 superfamily, is widely expressed in n-alkane-degrading bacteria. ![]()
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