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NAD-dependent dehydrogenases enable efficient growth of Paracoccus denitrificans on the PET monomer ethylene glycol

Author

Listed:
  • Minrui Ren

    (Leiden University)

  • Danni Li

    (Leiden University)

  • Holly Addison

    (Max Planck Institute for Terrestrial Microbiology)

  • Willem E. M. Noteborn

    (Leiden University)

  • Elisabeth H. Andeweg

    (Leiden University Medical Center)

  • Timo Glatter

    (Max Planck Institute for Terrestrial Microbiology)

  • Johannes H. Winde

    (Leiden University)

  • Johannes G. Rebelein

    (Max Planck Institute for Terrestrial Microbiology
    Philipps University Marburg)

  • Meindert H. Lamers

    (Leiden University Medical Center)

  • Lennart Schada von Borzyskowski

    (Leiden University)

Abstract

Ethylene glycol is a monomer of the plastic polyethylene terephthalate (PET) and an environmental pollutant of increasing concern. Although it is generally accepted that bacteria use ethylene glycol as growth substrate, not all involved enzymes are well understood. Here, we show that Paracoccus denitrificans assimilates ethylene glycol solely via NAD-dependent alcohol and aldehyde dehydrogenases. Using comparative proteomics, we identify a gene cluster that is strongly expressed in the presence of ethylene glycol. We report the functional and structural characterization of EtgB and EtgA, key enzymes encoded by this etg gene cluster. We furthermore show that the transcriptional activator EtgR controls expression of the gene cluster. Adaptive laboratory evolution on ethylene glycol results in faster growth, enabled by increased production of EtgB and EtgA. Bioinformatic analysis reveals that the etg gene cluster is widely distributed among bacteria, suggesting a common role of NAD-dependent dehydrogenases in microbial ethylene glycol assimilation.

Suggested Citation

  • Minrui Ren & Danni Li & Holly Addison & Willem E. M. Noteborn & Elisabeth H. Andeweg & Timo Glatter & Johannes H. Winde & Johannes G. Rebelein & Meindert H. Lamers & Lennart Schada von Borzyskowski, 2025. "NAD-dependent dehydrogenases enable efficient growth of Paracoccus denitrificans on the PET monomer ethylene glycol," Nature Communications, Nature, vol. 16(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-61056-x
    DOI: 10.1038/s41467-025-61056-x
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    References listed on IDEAS

    as
    1. Kathryn Tunyasuvunakool & Jonas Adler & Zachary Wu & Tim Green & Michal Zielinski & Augustin Žídek & Alex Bridgland & Andrew Cowie & Clemens Meyer & Agata Laydon & Sameer Velankar & Gerard J. Kleywegt, 2021. "Highly accurate protein structure prediction for the human proteome," Nature, Nature, vol. 596(7873), pages 590-596, August.
    2. Hongyuan Lu & Daniel J. Diaz & Natalie J. Czarnecki & Congzhi Zhu & Wantae Kim & Raghav Shroff & Daniel J. Acosta & Bradley R. Alexander & Hannah O. Cole & Yan Zhang & Nathaniel A. Lynd & Andrew D. El, 2022. "Machine learning-aided engineering of hydrolases for PET depolymerization," Nature, Nature, vol. 604(7907), pages 662-667, April.
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    4. Lennart Schada von Borzyskowski & Francesca Severi & Karen Krüger & Lucas Hermann & Alexandre Gilardet & Felix Sippel & Bianca Pommerenke & Peter Claus & Niña Socorro Cortina & Timo Glatter & Stefan Z, 2019. "Marine Proteobacteria metabolize glycolate via the β-hydroxyaspartate cycle," Nature, Nature, vol. 575(7783), pages 500-504, November.
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