Methionine Sulfoxide Reductases of Archaea
Open accessAbstract
Methionine sulfoxide reductases are found in all domains of life and are important in reversing the oxidative damage of the free and protein forms of methionine, a sulfur containing amino acid particularly sensitive to reactive oxygen species (ROS). Archaea are microbes of a domain of life distinct from bacteria and eukaryotes. Archaea are well known for their ability to withstand harsh environmental conditions that range from habitats of high ROS, such as hypersaline lakes of intense ultraviolet (UV) radiation and desiccation, to hydrothermal vents of low concentrations of dissolved oxygen at high temperature. Recent evidence reveals the methionine sulfoxide reductases of archaea function not only in the reduction of methionine sulfoxide but also in the ubiquitin-like modification of protein targets during oxidative stress, an association that appears evolutionarily conserved in eukaryotes. Here is reviewed methionine sulfoxide reductases and their distribution and function in archaea.
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Sousa, F. L., Thiergart, T., Landan, G., Nelson-Sathi, S., Pereira, I. A. C., Allen, J. F., Lane, N., & Martin, W. F. (2013) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0088 · Cited by 286 · cited 2× · see citing works
“Life evolved in an anaerobic world; thus, early archaea were relatively free from the damaging effects of ROS [27] and likely used a Wood–Ljungdahl pathway to generate energy and assimilate carbon (acetyl-CoA) from H2 and CO2 [28,29].”
UV and ionizing radiations induced DNA damage, differences and similarities
Ravanat, J.-L., & Douki, T. (2016) · Radiation Physics and Chemistry · doi:10.1016/j.radphyschem.2016.07.007 · Cited by 94 · see citing works
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- Authors
- Maupin-Furlow, J. A.
- Affiliations
- University of Florida (US)
- Corresponding author
- Maupin-Furlow, Julie A.
- Venue
- Antioxidants
- Publisher
- MDPI AG
- Published
- 2018-09-20
- Volume
- 7
- Issue
- 10
- Pages
- 124
- ISSN
- 2076-3921 (ISSN-L)
- PMC
- PMC6211008
- OpenAlex
- W2890693256
- Cited by
- 21
- References
- 2
- Citations by year
- 2026: 2 · 2025: 2 · 2023: 3 · 2022: 3 · 2021: 4 · 2020: 5 · 2019: 2
- FWCI
- 0.27
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- Antioxidants (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- JM-F through the Bilateral NSF/BIO-BBSRC program (NSF 1642283)
- the U.S. Department of Energy, Office of Basic Energy Sciences, Division of Chemical Sciences, Geosciences and Biosciences, Physical Biosciences Program (DOE DE-FG02-05ER15650)
- National Institutes of Health (NIH R01 GM57498)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- methionine sulfoxide reductase, archaea, oxidative stress, reactive oxygen species, methionine oxidation, ubiquitination, proteostasis, extremophiles, UV resistance, hydrothermal vents, desiccation tolerance, evolutionary conservation
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