Unknown

Dataset Information

0

UbiI, a new gene in Escherichia coli coenzyme Q biosynthesis, is involved in aerobic C5-hydroxylation.


ABSTRACT: Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multiple proteins. In this work, we show that the uncharacterized conserved visC gene is involved in Q biosynthesis in Escherichia coli, and we have renamed it ubiI. Based on genetic and biochemical experiments, we establish that the UbiI protein functions in the C5-hydroxylation reaction. A strain deficient in ubiI has a low level of Q and accumulates a compound derived from the Q biosynthetic pathway, which we purified and characterized. We also demonstrate that UbiI is only implicated in aerobic Q biosynthesis and that an alternative enzyme catalyzes the C5-hydroxylation reaction in the absence of oxygen. We have solved the crystal structure of a truncated form of UbiI. This structure shares many features with the canonical FAD-dependent para-hydroxybenzoate hydroxylase and represents the first structural characterization of a monooxygenase involved in Q biosynthesis. Site-directed mutagenesis confirms that residues of the flavin binding pocket of UbiI are important for activity. With our identification of UbiI, the three monooxygenases necessary for aerobic Q biosynthesis in E. coli are known.

SUBMITTER: Hajj Chehade M 

PROVIDER: S-EPMC3707705 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications


Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multiple proteins. In this work, we show that the uncharacterized conserved visC gene is involved in Q biosynthesis in Escherichia coli, and we have renamed it ubiI. Based on genetic and biochemical experiments, we establish that the UbiI protein functions in the C5-hydroxylation  ...[more]

Similar Datasets

| S-EPMC3911131 | biostudies-literature
| S-EPMC3070445 | biostudies-literature
| S-EPMC1636149 | biostudies-literature
| S-EPMC2943303 | biostudies-literature
| S-EPMC6070760 | biostudies-literature
| S-EPMC2755913 | biostudies-literature
| S-EPMC3337207 | biostudies-literature
| S-EPMC1785431 | biostudies-literature
| S-EPMC101899 | biostudies-literature
| S-EPMC3158064 | biostudies-literature