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© Research
Publication : The Journal of biological chemistry

The UbiK protein is an accessory factor necessary for bacterial ubiquinone (UQ) biosynthesis and forms a complex with the UQ biogenesis factor UbiJ

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Journal of biological chemistry - 30 May 2017

Loiseau L, Fyfe C, Aussel L, Hajj Chehade M, Hernández SB, Faivre B, Hamdane D, Mellot-Draznieks C, Rascalou B, Pelosi L, Velours C, Cornu D, Lombard M, Casadesús J, Pierrel F, Fontecave M, Barras F

Link to Pubmed [PMID] – 28559279

J. Biol. Chem. 2017 07;292(28):11937-11950

Ubiquinone (UQ), also referred to as coenzyme Q, is a widespread lipophilic molecule in both prokaryotes and eukaryotes in which it primarily acts as an electron carrier. Eleven proteins are known to participate in UQ biosynthesis in, and we recently demonstrated that UQ biosynthesis requires additional, nonenzymatic factors, some of which are still unknown. Here, we report on the identification of a bacterial gene,, which is required for efficient UQ biosynthesis, and which we have renamedUsing several methods, we demonstrated that the UbiK protein forms a complex with the C-terminal part of UbiJ, another UQ biogenesis factor we previously identified. We found that both proteins are likely to contribute to global UQ biosynthesis rather than to a specific biosynthetic step, because both ubiK and ubiJ mutants accumulated octaprenylphenol, an early intermediate of the UQ biosynthetic pathway. Interestingly, we found that both proteins are dispensable for UQ biosynthesis under anaerobiosis, even though they were expressed in the absence of oxygen. We also provide evidence that the UbiK-UbiJ complex interacts with palmitoleic acid, a major lipid inLast, in, ubiK was required for proliferation in macrophages and virulence in mice. We conclude that although the role of the UbiK-UbiJ complex remains unknown, our results support the hypothesis that UbiK is an accessory factor of Ubi enzymes and facilitates UQ biosynthesis by acting as an assembly factor, a targeting factor, or both.

https://www.ncbi.nlm.nih.gov/pubmed/28559279