Ergothioneine protects Streptomyces coelicolor A3(2) from oxidative stresses
Open accessAbstract
Thiol compounds with low-molecular weight, such as glutathione, mycothiol (MSH), bacillithiol, and ergothioneine (ERG), are known to protect microorganisms from oxidative stresses. Mycobacteria and actinobacteria utilize both MSH and ERG. The biological functions of MSH in mycobacteria have been extensively studied by genetic and biochemical studies, which have suggested it has critical roles for detoxification in cells. In contrast, the biological functions of ERG remain ambiguous because its biosynthetic genes were only recently identified in Mycobacterium avium. In this study, we constructed mutants of Streptomyces coelicolor A3(2), in which either the MSH or ERG biosynthetic gene was disrupted, and examined their phenotypes. A mshC (SCO1663)-disruptant completely lost MSH productivity. In contrast, a disruptant of the egtA gene (SCO0910) encoding γ-glutamyl-cysteine synthetase unexpectedly retained reduced productivity of ERG, probably because of the use of l-cysteine instead of γ-glutamyl-cysteine. Both disruptants showed delayed growth at the late logarithmic phase and were more susceptible to hydrogen peroxide and cumene hydroperoxide than the parental strain. Interestingly, the ERG-disruptant, which still kept reduced ERG productivity, was more susceptible. Furthermore, the ERG-disruptant accumulated 5-fold more MSH than the parental strain. In contrast, the amount of ERG was almost the same between the MSH-disruptant and the parental strain. Taken together, our results suggest that ERG is more important than MSH in S. coelicolor A3(2).
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In M. tuberculosis and other mycobacteria, other actinobacteria and fungi, ERG can have a role as an antioxidant and act as a buffer against reductive stress.
“In M. tuberculosis and other mycobacteria(254), and also in other actinobacteria(255) and in fungi(247,256,257), it is clear that ERG can have a role as an antioxidant(66,258–260) and also act as a buffer against reductive stress(261).”
From The biology of ergothioneine, an antioxidant nutraceutical (2020) · cites this paper as [255]
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- Authors
- Nakajima, S., Satoh, Y., Yanashima, K., Matsui, T., & Dairi, T.
- Affiliations
- Hokkaido University (JP)
- Corresponding author
- Dairi, Tohru
- Venue
- Journal of Bioscience and Bioengineering
- Publisher
- Elsevier BV
- Published
- 2015-09
- Volume
- 120
- Issue
- 3
- Pages
- 294-298
- ISSN
- 1347-4421 (ISSN-L)
- 1389-1723
- OpenAlex
- W2159104220
- Cited by
- 38
- References
- 23
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 2 · 2023: 6 · 2022: 1 · 2021: 1 · 2020: 5 · 2019: 3 · 2018: 4 · 2017: 7 · 2016: 1 · 2015: 1
- FWCI
- 2.17
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- cc-by-nc-nd
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- Locations
- Journal of Bioscience and Bioengineering (publishedVersion)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion, cc-by-nc-nd)
- Hokkaido University Collection of Scholarly and Academic Papers (Hokkaido University) (submittedVersion, cc-by-nc-nd)
- Funders
- Japan Society for the Promotion of Science (24651235)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- ergothioneine, mycothiol, Streptomyces coelicolor A3(2), oxidative stress, thiols, EGTA, gamma-glutamylcysteine synthetase, hydrogen peroxide susceptibility, cumene hydroperoxide, actinobacteria, cysteine
- MeSH terms
- Cysteine, Ergothioneine, Glutamate-Cysteine Ligase, Glycopeptides, Hydrogen Peroxide, Inositol, Oxidative Stress, Streptomyces coelicolor
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