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A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans

Author

Listed:
  • Limin Liu

    (Howard Hughes Medical Institute
    Department of Medicine, Pulmonary and Cardiology Divisions)

  • Alfred Hausladen

    (Department of Medicine, Pulmonary and Cardiology Divisions)

  • Ming Zeng

    (Department of Medicine, Pulmonary and Cardiology Divisions)

  • Loretta Que

    (Department of Medicine, Pulmonary and Cardiology Divisions)

  • Joseph Heitman

    (Howard Hughes Medical Institute
    Duke University Medical Center)

  • Jonathan S. Stamler

    (Howard Hughes Medical Institute
    Department of Medicine, Pulmonary and Cardiology Divisions
    Duke University Medical Center)

Abstract

Considerable evidence indicates that NO biology involves a family of NO-related molecules and that S-nitrosothiols (SNOs) are central to signal transduction and host defence1,2,3,4,5. It is unknown, however, how cells switch off the signals or protect themselves from the SNOs produced for defence purposes. Here we have purified a single activity from Escherichia coli, Saccharomyces cerevisiae and mouse macrophages that metabolizes S-nitrosoglutathione (GSNO), and show that it is the glutathione-dependent formaldehyde dehydrogenase. Although the enzyme is highly specific for GSNO, it controls intracellular levels of both GSNO and S-nitrosylated proteins. Such ‘GSNO reductase’ activity is widely distributed in mammals. Deleting the reductase gene in yeast and mice abolishes the GSNO-consuming activity, and increases the cellular quantity of both GSNO and protein SNO. Furthermore, mutant yeast cells show increased susceptibility to a nitrosative challenge, whereas their resistance to oxidative stress is unimpaired. We conclude that GSNO reductase is evolutionarily conserved from bacteria to humans, is critical for SNO homeostasis, and protects against nitrosative stress.

Suggested Citation

  • Limin Liu & Alfred Hausladen & Ming Zeng & Loretta Que & Joseph Heitman & Jonathan S. Stamler, 2001. "A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans," Nature, Nature, vol. 410(6827), pages 490-494, March.
    • Handle: RePEc:nat:nature:v:410:y:2001:i:6827:d:10.1038_35068596
    DOI: 10.1038/35068596
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    Cited by:

    1. Mutian Jia & Li Chai & Jie Wang & Mengge Wang & Danhui Qin & Hui Song & Yue Fu & Chunyuan Zhao & Chengjiang Gao & Jihui Jia & Wei Zhao, 2024. "S-nitrosothiol homeostasis maintained by ADH5 facilitates STING-dependent host defense against pathogens," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Takeshi Haseba & Youkichi Ohno, 2010. "A New View of Alcohol Metabolism and Alcoholism—Role of the High- K m Class Ⅲ Alcohol Dehydrogenase (ADH3)," IJERPH, MDPI, vol. 7(3), pages 1-17, March.
    3. Roby Greenwald & Anne M Fitzpatrick & Benjamin Gaston & Nadzeya V Marozkina & Serpil Erzurum & W Gerald Teague, 2010. "Breath Formate Is a Marker of Airway S-Nitrosothiol Depletion in Severe Asthma," PLOS ONE, Public Library of Science, vol. 5(7), pages 1-6, July.
    4. D. Procházková & D. Haisel & D. Pavlíková, 2014. "Nitric oxide biosynthesis in plants - the short overview," Plant, Soil and Environment, Czech Academy of Agricultural Sciences, vol. 60(3), pages 129-134.
    5. Jonathan L Robinson & Mark P Brynildsen, 2013. "A Kinetic Platform to Determine the Fate of Nitric Oxide in Escherichia coli," PLOS Computational Biology, Public Library of Science, vol. 9(5), pages 1-1, May.

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