ArticleMethods in enzymology2021
Thermococcus kodakarensis provides a versatile hyperthermophilic archaeal platform for protein expression.
Article in Methods in enzymology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- Archaeal family B DNA polymerase facilitates lagging strand DNA replication in the Thermococcales.Nucleic acids research · 2026Article
- Evolution and Functional Implications of Codon Usage Bias in Eukaryotes.Journal of molecular evolution · 2026Review
- Rerouting reductant flux via protein tethering enhances biohydrogen production in Thermococcus kodakarensis.Applied microbiology and biotechnology · 2026Article
- The Thermococcales as a model system: historical perspectives and emerging tools.Journal of bacteriology · 2025Review
- Kinetic characterization of RNA synthesis catalyzed by the model hyperthermophilic archaeonmSphere · 2025Article
- A dynamic protein interactome drives energy conservation and electron flux inApplied and environmental microbiology · 2025Article
- Comprehensive nucleoside analysis of archaeal RNA modification profiles reveals an mCell reports · 2025Article
- Advancing archaeal research through FAIR resource and data sharing, and inclusive community building.Communications biology · 2025Review
- Unravelling Prokaryotic Codon Usage: Insights from Phylogeny, Influencing Factors and Pathogenicity.Current genomics · 2025Review
- A novelProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Advances in Extremophile Research: Biotechnological Applications through Isolation and Identification Techniques.Life (Basel, Switzerland) · 2024Review
- The extensive mNature communications · 2024Article
- Identification of two archaeal GDGT lipid-modifying proteins reveals diverse microbes capable of GMGT biosynthesis and modification.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Tetraether archaeal lipids promote long-term survival in extreme conditions.Molecular microbiology · 2024Article
- Archaea as a Model System for Molecular Biology and Biotechnology.Biomolecules · 2023Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Hyperthermophiles, typically defined as organisms with growth optima ≥80°C, are dominated by the Archaea. Proteins that support life at the extremes of temperatures often retain substantial biotechnological and commercial value, but the recombinant expression of individual hyperthermophilic proteins is commonly complicated in non-native mesophilic hosts due to differences in codon bias, intracellular solutes and the requirement for accessory factors that aid in folding or deposition of metal centers within archaeal proteins. The development of versatile protein expression and facilitated protein purification systems in the model, genetically tractable, hyperthermophilic marine archaeon Thermococcus kodakarensis provides an attractive platform for protein expression within the hyperthermophiles. The assortment of T. kodakarensis genetic backgrounds and compatible selection markers allow iterative genetic manipulations that facilitate protein overexpression and expedite protein purifications. Expression vectors that stably replicate both in T. kodakarensis and Escherichia coli have been validated and permit high-level ectopic gene expression from a variety of controlled and constitutive promoters. Biologically relevant protein associations can be maintained during protein purifications to identify native protein partnerships and define protein interaction networks. T. kodakarensis thus provides a versatile platform for the expression and purification of thermostable proteins.
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