Atomi et al, 2004
T. kodakarensis was isolated from a solfatara near the shore of Kodakara Island, Kagoshima, Japan. The isolate was originally named Pyrococcus kodakarensis KOD1, but reclassified as a species of Thermococcus, based on 16S rRNA sequence. Early research with T. kodakarensis was directed mostly at its thermostable enzymes, 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.
T. 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 di-ether and tetra-ether lipids, and an outer glycoprotein coat. 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. 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. Growth is possible at temperature ranging from 60–100 °C, with an optimum at 85 °C. Like other marine organisms, high salt concentrations are required for optimal growth, and cell lysis may occur in dilute solutions.
In 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.
- Atomi, H., T. Fukui, T. Kanai, M. Morikawa, and T. Imanaka. 2004. Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1. Archaea 1:263–267.
- Morikawa, M., Y. Izawa, N. Rashid, T. Hoaki, and T. Imanaka. 1994. Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp. Applied and Environmental Microbiology 60:4559–4566.
- Sato, T., T. Fukui, H. Atomi, and T. Imanaka. 2003. Targeted Gene Disruption by Homologous Recombination in the Hyperthermophilic Archaeon Thermococcus kodakaraensis KOD1. Journal of Bacteriology 185:210–220.
- Sato, T., T. Fukui, H. Atomi, and T. Imanaka. 2005. Improved and Versatile Transformation System Allowing Multiple Genetic Manipulations of the Hyperthermophilic Archaeon Thermococcus kodakaraensis. Applied and Environmental Microbiology 71:3889–3899. Genome Research 15:352–363.
- Fukui, T., H. Atomi, T. Kanai, R. Matsumi, S. Fujiwara, and T. Imanaka. 2005. Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Research 15:352–363.
Elshawadfy, Ashraf M.; Keith, Brian J.; Ooi, H'Ng Ee; Kinsman, Thomas; Heslop, Pauline; Connolly, Bernard A. (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 (00224). doi:10.3389/fmicb.2014.00224.
Hwa, Kuo-Yuan; Subramani, Boopathi; Shen, San-Tai; Lee, Yu-May (March 27, 2014). "An intermolecular disulfide bond is required for thermostability and thermoactivity of β-glycosidase from Thermococcus kodakarensis KOD1". Applied microbiology and biotechnology. 98 (18): 7825–7836. doi:10.1007/s00253-014-5731-6.
Kishimoto, Asako; Kita, Akiko; Ishibashi, Takuya; Tomita, Hiroya; Yokooji, Yuusuke; Imanaka, Tadayuki; Atomi, Haruyuki; Miki, Kunio (September 2014). "Crystal structure of phosphopantothenate synthetase from Thermococcus kodakarensis". Proteins Structure Function and Bioinformatics. 82 (9): 1924–1936. doi:10.1002/prot.24546. PMID 24638914. Retrieved 10 November 2014.