Thermococcus kodakarensis is a species of thermophilic archaea. The type strain T. kodakarensis KOD1 is one of the best-studied members of the genus.[2]
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| Species: | T. kodakarensis
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| Thermococcus kodakarensis Atomi et al, 2004[1]
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History
editT. kodakarensis was isolated from a solfatara near the shore of Kodakara Island, Kagoshima, Japan.[3] The isolate was originally named Pyrococcus kodakarensis KOD1, but reclassified as a species of Thermococcus, based on 16S rRNA sequence.[1] Early research with T. kodakarensis was directed mostly at its thermostable enzymes (like the KOD DNA polymerase), but its relative ease of handling and genetic manipulation facilitated by natural competence has made it an attractive system for the study of several biological processes.[4][5]
Properties
editT. kodakarensis cells are irregular cocci 1–2 μm in diameter, often occurring in pairs, and are highly motile by means of lophotrichous archaella. The cell wall consists of a layer of diether and tetraether lipids, and an outer glycoprotein coat.[1][3] T. kodakarensis is an obligate anaerobe, and a heterotroph, growing rapidly on a variety of organic substrates in the presence of elemental sulfur, producing hydrogen sulfide gas. The generation time is estimated to be 40 minutes under optimum conditions.[3] The requirement for elemental sulfur is relieved when pyruvate or starch is used for growth. In the absence of sulfur, hydrogen is produced instead of hydrogen sulfide.[1] Growth is possible at temperature ranging from 60–100 °C, with an optimum at 85 °C.[1] Like other marine organisms, high salt concentrations are required for optimal growth, and cell lysis may occur in dilute solutions.
Genome
editIn 2005, the genome of T. kodakarensis KOD1 was fully sequenced. The genome consists of a single 2,088,737 base pair circular chromosome, encoding a predicted 2306 proteins.[6]
See also
editReferences
edit- ^ a b c d e Atomi H, Fukui T, Kanai T, Morikawa M, Imanaka T (October 2004). "Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1". Archaea. 1 (4): 263–7. doi:10.1155/2004/204953. PMC 2685570. PMID 15810436.
- ^ Atomi H, Reeve J (November 2019). "Microbe Profile: Thermococcus kodakarensis: the model hyperthermophilic archaeon". Microbiology. 165 (11): 1166–1168. doi:10.1099/mic.0.000839. PMC 7137780. PMID 31436525.
- ^ a b c Morikawa M, Izawa Y, Rashid N, Hoaki T, Imanaka T (December 1994). "Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp". Applied and Environmental Microbiology. 60 (12): 4559–66. doi:10.1128/aem.60.12.4559-4566.1994. PMC 202019. PMID 7811092.
- ^ Sato T, Fukui T, Atomi H, Imanaka T (January 2003). "Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1". Journal of Bacteriology. 185 (1): 210–20. doi:10.1128/JB.185.1.210-220.2003. PMC 141832. PMID 12486058.
- ^ Sato T, Fukui T, Atomi H, Imanaka T (July 2005). "Improved and versatile transformation system allowing multiple genetic manipulations of the hyperthermophilic archaeon Thermococcus kodakaraensis". Applied and Environmental Microbiology. 71 (7): 3889–99. doi:10.1128/AEM.71.7.3889-3899.2005. PMC 1169065. PMID 16000802.
- ^ Fukui T, Atomi H, Kanai T, Matsumi R, Fujiwara S, Imanaka T (March 2005). "Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes". Genome Research. 15 (3): 352–63. doi:10.1101/gr.3003105. PMC 551561. PMID 15710748.
Further reading
edit- Elshawadfy AM, Keith BJ, Ee Ooi H, Kinsman T, Heslop P, Connolly BA (27 May 2014). "DNA polymerase hybrids derived from the family-B enzymes of Pyrococcus furiosus and Thermococcus kodakarensis: improving performance in the polymerase chain reaction". Frontiers in Microbiology. 5 (224): 224. doi:10.3389/fmicb.2014.00224. PMC 4034419. PMID 24904539.
- Hwa KY, Subramani B, Shen ST, Lee YM (September 2014). "An intermolecular disulfide bond is required for thermostability and thermoactivity of β-glycosidase from Thermococcus kodakarensis KOD1". Applied Microbiology and Biotechnology. 98 (18): 7825–36. doi:10.1007/s00253-014-5731-6. PMID 24728717. S2CID 9812474.
- Kishimoto A, Kita A, Ishibashi T, Tomita H, Yokooji Y, Imanaka T, et al. (September 2014). "Crystal structure of phosphopantothenate synthetase from Thermococcus kodakarensis". Proteins. 82 (9): 1924–36. doi:10.1002/prot.24546. PMID 24638914. S2CID 23549563.