ArticleApplied microbiology and biotechnology2024
A mycofactocin-associated dehydrogenase is essential for ethylene glycol metabolism by Rhodococcus jostii RHA1.
Article in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 22 citations in OpenAlex.
- From screening to sequencing: Investigating the monoethylene glycol (MEG) biodegradation byBiotechnology reports (Amsterdam, Netherlands) · 2026Article
- Elucidating biodegradation of dimethyl terephthalate by twoMetabolic engineering communications · 2026Article
- NAD-dependent dehydrogenases enable efficient growth of Paracoccus denitrificans on the PET monomer ethylene glycol.Nature communications · 2025Article
- MftG is crucial for ethanol metabolism of mycobacteria by linking mycofactocin oxidation to respiration.eLife · 2025Article
- From plastic waste to bioprocesses: Using ethylene glycol from polyethylene terephthalate biodegradation to fuelMetabolic engineering communications · 2024Article
- The catabolism of ethylene glycol byApplied and environmental microbiology · 2024Article
- Novel aspects of ethylene glycol catabolism.Applied microbiology and biotechnology · 2024Review
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3 authors at 2 institutions in 1 country.
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Abstract
Ethylene glycol is an industrially important diol in many manufacturing processes and a building block of polymers, such as poly(ethylene terephthalate). In this study, we found that a mycolic acid-containing bacterium Rhodococcus jostii RHA1 can grow with ethylene glycol as a sole source of carbon and energy. Deletion of a putative glycolate dehydrogenase gene (RHA1_ro03227) abolished growth with ethylene glycol, indicating that ethylene glycol is assimilated via glycolate in R. jostii RHA1. Transcriptome sequencing and gene deletion analyses revealed that a gene homologous to mycofactocin (MFT)-associated dehydrogenase (RHA1_ro06057), hereafter referred to as EgaA, is essential for ethylene glycol assimilation. Furthermore, egaA deletion also negatively affected the utilization of ethanol, 1-propanol, propylene glycol, and 1-butanol, suggesting that EgaA is involved in the utilization of various alcohols in R. jostii RHA1. Deletion of MFT biosynthetic genes abolished growth with ethylene glycol, indicating that MFT is the physiological electron acceptor of EgaA. Further genetic studies revealed that a putative aldehyde dehydrogenase (RHA1_ro06081) is a major aldehyde dehydrogenase in ethylene glycol metabolism by R. jostii RHA1. KEY POINTS: • Rhodococcus jostii RHA1 can assimilate ethylene glycol via glycolate • A mycofactocin-associated dehydrogenase is involved in the oxidation of ethylene glycol • An aldehyde dehydrogenase gene is important for the ethylene glycol assimilation.
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