Thermococcus

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Thermococcus
Scientific classification
Domain:
Archaea
Kingdom:
Euryarchaeota
Phylum:
Euryarchaeota
Class:
Thermococci
Order:
Thermococcales
Family:
Thermococcaceae
Genus:
Thermococcus

Zillig 1983
Type species
Thermococcus celer
Zillig 1983
Species

See text

In taxonomy, Thermococcus is a genus of thermophilic Archaea in the family the Thermococcaceae. [1]

Contents

Members of the genus Thermococcus are typically irregularly shaped coccoid species, ranging in size from 0.6 to 2.0 μm in diameter. [2] Some species of Thermococcus are immobile, and some species have motility, using flagella as their main mode of movement.[ citation needed ] These flagella typically exist at a specific pole of the organism.[ citation needed ] This movement has been seen at room or at high temperatures, depending on the specific organism. [3] In some species, these microorganisms can aggregate and form white-gray plaques. [4] Species under Thermococcus typically thrive at temperatures between 60 and 105 °C, [5] either in the presence of black smokers (hydrothermal vents), or freshwater springs. [6] Species in this genus are strictly anaerobes, [7] [8] and are thermophilic, [2] [7] found in a variety depths, such as in hydrothermal vents 2500m below the ocean surface, [9] but also centimeters below the water surface in geothermal springs. [10] These organisms thrive at pH levels of 5.6-7.9. [11] Members of this genus have been found in many hydrothermal vent systems in the world, including from the seas of Japan, [12] to off the coasts of California. [13] Sodium Chloride salt is typically present in these locations at 1%-3% concentration, [8] but is not a required substrate for these organisms, [14] [15] as one study showed Thermococcus members living in fresh hot water systems in New Zealand, [6] but they do require a low concentration of lithium ions for growth. [16] Thermococcus members are described as heterotrophic, chemotrophic, [2] [17] [18] and are organotrophic sulfanogens; using elemental sulfur and carbon sources including amino acids, carbohydrates, and organic acids such as pyruvate. [17] [18] [19]

Phylogeny

16S rRNA based LTP_08_2023 [20] [21] [22] GTDB 08-RS214 by Genome Taxonomy Database. [23] [24] [25]
Thermococcus

T. aggregans

T. aegaeusArab et al. 2000

T. alcaliphilus

T. litoralis Neuner et al. 2001

T. argininiproducensPark et al. 2023

T. sibiricus

species‑group 2

Pyrococcus

Thermococcus s.s.

T. barophilus

T. paralvinellae

T. acidaminovoransDirmeier et al. 2001

T. gorgonarius

T. fumicolansGodfroy et al. 1996

T. pacificus

T. waiotapuensisGonzlez et al. 2001

T. zilligii

T. guaymasensis

T. eurythermalis

T. henrietii

T. nautili

T. gammatolerans

T. kodakarensis

T. peptonophilus

T. stetteri

T. cleftensis

T. siculi

T. indicus

T. celericrescens

T. aciditoleransLi et al. 2021

T. camini

T. profundus

T. piezophilus

T. coalescensKuwabara et al. 2005

T. prieuriiGorlas et al. 2013

T. thioreducens

T. hydrothermalis Godfroy et al. 1997

T. barossii

T. atlanticusCambon-Bonavita et al. 2004

T. celer

Thermococcus

T. sibiricusMiroshnichenko et al. 2001

T. aggregansCanganella et al. 1998

T. alcaliphilus Keller et al. 1997

"T. bergensis" Birkeland et al. 2021

species‑group 2
Thermococcus

T. barophilus Marteinsson et al. 1999

T. paralvinellaeHensley et al. 2014

species‑group 3

Pyrococcus

Thermococcus s.s.

T. gammatolerans Jolivet et al. 2003

T. guaymasensisCanganella et al. 1998

T. eurythermalisZhao et al. 2015

T. henrietiiAlain et al. 2021

T. nautiliSoler et al. 2007

T. stetteri Miroshnichenko 1990

T. kodakarensis Atomi et al. 2005

T. peptonophilus González et al. 1996

T. profundus Kobayashi and Horikoshi 1995

T. gorgonariusMiroshnichenko et al. 1998

T. zilligiiRonimus et al. 1999

"T. onnurineus" Bae et al. 2006

T. piezophilusDalmasso et al. 2017

T. celer Zillig 1983 (type sp.)

T. barossiiDuffaud et al. 2005

"T. radiotolerans" Jolivet et al. 2004

T. thioreducensPikuta et al. 2007

T. cleftensisHensley et al. 2014

T. pacificusMiroshnichenko et al. 1998

T. siculiGrote et al. 2000

T. indicusLim et al. 2021

T. caminiCourtine et al. 2021

T. celericrescensKuwabara et al. 2007

Unassigned species:

Metabolism

Metabolically, Thermococcus spp. have developed a different form of glycolysis from eukaryotes and prokaryotes. [26] [5] One example of a metabolic pathway for these organisms is the metabolism of peptides, [26] which occurs in three steps: first, hydrolysis of the peptides to amino acids is catalyzed by peptidases, [5] then the conversion of the amino acids to keto acids is catalyzed by aminotransferases, [26] and finally CO2 is released from the oxidative decarboxylation or the keto acids by four different enzymes, [5] which produces coenzyme A derivatives that are used in other important metabolic pathways. [5] Thermococcus species also have the enzyme rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), [27] which is made from enzymes involved in the metabolism of nucleic acids in Thermococcus kodakarensis, [5] [26] [27] showing how integrated these metabolic systems truly are for these hyperthermophilic microorganisms. [27] Some nutrients are limiting in Thermococcus cell growth. [27] Nutrients that affect cell growth the most in thermococcal species are carbon and nitrogen sources. [27] Since thermococcal species do not metabolically generate all necessary amino acids, some have to be provided by the environment in which these organisms thrive. Some of these needed amino acids are leucine, isoleucine, and valine (the branched-chain amino acids). [27] When Thermococcus species are supplemented with these amino acids, they can metabolize them and produce acetyl-CoA or succinyl-CoA, [27] which are important precursors used in other metabolic pathways essential for cellular growth and respiration. [27] Thermococcus onnurineus lacks the genes for purine nucleotide biosynthesis and thus relies on environmental sources to meet its purine requirements. [28] With today's technology, Thermococcus members are relatively easy to grow in labs, [29] and are therefore considered model organisms for studying the physiological and molecular pathways of extremophiles. [30] [31] Thermococcus kodakarensis is one example of a model Thermococcus species, a microorganism in which has had its entire genome examined and replicated. [31] [32] [33]

Ecology

Thermococcal species can grow between 60 and 102 °C,optimal temperature at 85 °C which gives them a great ecological advantage to be the first organisms to colonize new hydrothermal environments. [5] [34] [35] As hyperthermophiles, there is a need for extreme environmental conditions, including temperature, pH, and salt. These conditions lead to the production of stress proteins and molecular chaperones that protect DNA as well as housekeeping cellular machinery. Thermococcus also thrives under gluconeogenic conditions. Some thermococcal species produce CO2, H2, and H2S as products of metabolism and respiration. [31] The releases of these molecules are then used by other autotrophic species, aiding the diversity of hydrothermal microbial communities. [5] This type of continuous enrichment culture plays a crucial role in the ecology of deep-sea hydrothermal vents, [36] suggesting that thermococci interact with other organisms via metabolite exchange, which supports the growth of autotrophs. [5] Thermococcus species that release H2 with the use of multiple hydrogenases (including CO-dependent hydrogenases) have been regarded as potential biocatalysts for water-gas shift reactions. [37]

Transportation mechanisms

Thermococcus species are naturally competent in taking up DNA and incorporating donor DNA into their genomes via homologous recombination. [38] These species can produce membrane vesicles (MVs), [38] formed by budding from the outermost cellular membranes, [38] [39] which can capture and obtain plasmids from neighboring Archaea species to transfer the DNA into either themselves or surrounding species. [38] These MVs are secreted from the cells in clusters, forming nanospheres or nanotubes, [39] keeping the internal membranes continuous. [38] Competence for DNA transfer and integration of donor DNA into the recipient genome by homologous recombination is common in the archaea and appears to be an adaptation for repairing DNA damage in the recipient cells (see Archaea subsection "Gene transfer and genetic exchange").

Thermococcus species produce numerous MVs, transferring DNA, metabolites, and even toxins in some species; [39] moreover, these MVs protect their contents against thermodegradation by transferring these macromolecules in a protected environment. [38] [39] MVs also prevent infections by capturing viral particles. [39] Along with transporting macromolecules, Thermococcus species use MVs to communicate to each other. [38] Furthermore, these MVs are used by a specific species (Thermococcus coalescens) to indicate when aggregation should occur, [38] so these typically single-celled miroorganisms can fuse into one massive single cell. [38]

It has been reported that Thermococcus kodakarensis has four virus-like integrated gene elements containing subtilisin-like serine protease precursors. [40] To date, only two viruses have been isolated from Thermococcus spp., PAVE1 and TPV1. [40] These viruses exist in their hosts in a carrier state. [40]
The process of DNA replication and elongation has been extensively studied in T. kodakarensis. [40] The DNA molecule is a circular structure consisting of about 2 million base pairs in length, and has more than 2,000 sequences that code for proteins. [40]

Future technology

An enzyme from Thermococcus, Tpa-S DNA polymerase, has been found to be more efficient in long and rapid polymerase chain reaction (PCR) than Taq polymerase. [41] Tk-SP, another enzyme from T. kodakarensis, [41] [42] can degrade abnormal prion proteins (PrPSc); [41] prions are misfolded proteins that can cause fatal diseases in all organisms. [41] Tk-SP shows broad substrate specificity, and degraded prions exponentially in the lab setting. [41] This enzyme does not require calcium or any other substrate to fold, so is showing great potential in studies this far. [41] Additional studies have been coordinated on the phosphoserine phosphatase (PSP) enzyme of T. onnurineus, which provided an essential component in the regulation of PSP activity. [42] This information is useful for drug companies, because abnormal PSP activity leads to a major decrease in serine levels of the nervous system, causing neurological diseases and complications. [42]

Thermococcus spp. can increase gold mining efficiency up to 95% due to their specific abilities in bioleaching. [43]

See also

Related Research Articles

<span class="mw-page-title-main">Extremophile</span> Organisms capable of living in extreme environments

An extremophile is an organism that is able to live in extreme environments, i.e., environments with conditions approaching or stretching the limits of what known life can adapt to, such as extreme temperature, radiation, salinity, or pH level.

<span class="mw-page-title-main">Thermophile</span> Organism that thrives at relatively high temperatures

A thermophile is an organism—a type of extremophile—that thrives at relatively high temperatures, between 41 and 122 °C. Many thermophiles are archaea, though some of them are bacteria and fungi. Thermophilic eubacteria are suggested to have been among the earliest bacteria.

A hyperthermophile is an organism that thrives in extremely hot environments—from 60 °C (140 °F) upwards. An optimal temperature for the existence of hyperthermophiles is often above 80 °C (176 °F). Hyperthermophiles are often within the domain Archaea, although some bacteria are also able to tolerate extreme temperatures. Some of these bacteria are able to live at temperatures greater than 100 °C, deep in the ocean where high pressures increase the boiling point of water. Many hyperthermophiles are also able to withstand other environmental extremes, such as high acidity or high radiation levels. Hyperthermophiles are a subset of extremophiles. Their existence may support the possibility of extraterrestrial life, showing that life can thrive in environmental extremes.

<span class="mw-page-title-main">Archaeoglobaceae</span> Family of archaea

Archaeoglobaceae are a family of the Archaeoglobales. All known genera within the Archaeoglobaceae are hyperthermophilic and can be found near undersea hydrothermal vents. Archaeoglobaceae are the only family in the order Archaeoglobales, which is the only order in the class Archaeoglobi.

<i>Pyrococcus furiosus</i> Species of archaeon

Pyrococcus furiosus is a heterotrophic, strictly anaerobic, extremophilic, model species of archaea. It is classified as a hyperthermophile because it thrives best under extremely high temperatures, and is notable for having an optimum growth temperature of 100 °C. P. furiosus belongs to the Pyrococcus genus, most commonly found in extreme environmental conditions of hydrothermal vents. It is one of the few prokaryotic organisms that has enzymes containing tungsten, an element rarely found in biological molecules.

Caldococcus is a genus of Archaea in the order Desulfurococcales.

Thermococcus litoralis is a species of Archaea that is found around deep-sea hydrothermal vents as well as shallow submarine thermal springs and oil wells. It is an anaerobic organotroph hyperthermophile that is between 0.5–3.0 μm (20–118 μin) in diameter. Like the other species in the order thermococcales, T. litoralis is an irregular hyperthermophile coccus that grows between 55–100 °C (131–212 °F). Unlike many other thermococci, T. litoralis is non-motile. Its cell wall consists only of a single S-layer that does not form hexagonal lattices. Additionally, while many thermococcales obligately use sulfur as an electron acceptor in metabolism, T. litoralis only needs sulfur to help stimulate growth, and can live without it. T. litoralis has recently been popularized by the scientific community for its ability to produce an alternative DNA polymerase to the commonly used Taq polymerase. The T. litoralis polymerase, dubbed the vent polymerase, has been shown to have a lower error rate than Taq but due to its proofreading 3’–5’ exonuclease abilities.

Thermococcus celer is a Gram-negative, spherical-shaped archaeon of the genus Thermococcus. The discovery of T. celer played an important role in rerooting the tree of life when T. celer was found to be more closely related to methanogenic Archaea than to other phenotypically similar thermophilic species. T. celer was the first archaeon discovered to house a circularized genome. Several type strains of T. celer have been identified: Vu13, ATCC 35543, and DSM 2476.

<i>Thermococcus gammatolerans</i> Species of archaeon

Thermococcus gammatolerans is an archaea extremophile and the most radiation-resistant organism known to exist.

Methanocaldococcus jannaschii is a thermophilic methanogenic archaean in the class Methanococci. It was the first archaeon, and third organism, to have its complete genome sequenced. The sequencing identified many genes unique to the archaea. Many of the synthesis pathways for methanogenic cofactors were worked out biochemically in this organism, as were several other archaeal-specific metabolic pathways.

Thermococcus kodakarensis is a species of thermophilic archaea. The type strain T. kodakarensis KOD1 is one of the best-studied members of the genus.

Pyrococcus abyssi is a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent in the North Fiji Basin at 2,000 metres (6,600 ft). It is anaerobic, sulfur-metabolizing, gram-negative, coccus-shaped and highly motile. Its optimum growth temperature is 96 °C (205 °F). Its type strain is GE5. Pyrococcus abyssi has been used as a model organism in studies of DNA polymerase. This species can also grow at high cell densities in bioreactors.

Thermoplasma volcanium is a moderate thermoacidophilic archaea isolated from acidic hydrothermal vents and solfatara fields. It contains no cell wall and is motile. It is a facultative anaerobic chemoorganoheterotroph. No previous phylogenetic classifications have been made for this organism. Thermoplasma volcanium reproduces asexually via binary fission and is nonpathogenic.

Thermococcus profundus is a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent. It is coccoid-shaped with 1–2 μm in diameter, designated as strain DT5432.

Thermococcus chitonophagus is a chitin-degrading, hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent. It is anaerobic, round to slightly irregular coccus-shaped, 1.2–2.5 μm in diameter, and motile by means of a tuft of flagella.

Persephonella marina is a Gram-negative, rod shaped bacteria that is a member of the Aquificota phylum. Stemming from Greek, the name Persephonella is based upon the mythological goddess Persephone. Marina stems from a Latin origin, meaning "belonging to the sea". It is a thermophile with an obligate chemolithoautotrophic metabolism. Growth of P. marina can occur in pairs or individually, but is rarely seen aggregating in large groups. The organism resides on sulfidic chimneys in the deep ocean and has never been documented as a pathogen.

Thermococcus barophilus is a piezophilic and hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent. It is anaerobic and sulfur-metabolising, with type strain MPT.

Thermococcus peptonophilus is a fast-growing hyperthermophilic archaeon. It is coccus-shaped, obligately anaerobic and about 0.7–2 μm in diameter. It is a strict anaerobe and grows exclusively on complex substrates, such as peptone, casein, tryptone, and yeast extract. It cannot use carbon dioxide as a source of carbon. Although it can grow somewhat in the absence of elemental sulfur, it prefers sulfur.

Saccharolobus solfataricus is a species of thermophilic archaeon. It was transferred from the genus Sulfolobus to the new genus Saccharolobus with the description of Saccharolobus caldissimus in 2018.

Methanocaldococcussp. FS406-22 is an archaea in the genus Methanocaldococcus. It is an anaerobic, piezophilic, diazotrophic, hyperthermophilic marine archaeon. This strain is notable for fixing nitrogen at the highest known temperature of nitrogen fixers recorded to date. The 16S rRNA gene of Methanocaldococcus sp. FS406-22, is almost 100% similar to that of Methanocaldococcus jannaschii, a non-nitrogen fixer.

References

  1. ↑ See the NCBI webpage on Thermococcus. Data extracted from the "NCBI taxonomy resources". National Center for Biotechnology Information . Retrieved 2007-03-19.
  2. 1 2 3 Canganella F, Jones WJ, Gambacorta A, Antranikian G (October 1998). "Thermococcus guaymasensis sp. nov. and Thermococcus aggregans sp. nov., two novel thermophilic archaea isolated from the Guaymas Basin hydrothermal vent site". International Journal of Systematic Bacteriology. 48 Pt 4 (4): 1181–5. doi: 10.1099/00207713-48-4-1181 . PMID   9828419.
  3. ↑ Tagashira K, Fukuda W, Matsubara M, Kanai T, Atomi H, Imanaka T (January 2013). "Genetic studies on the virus-like regions in the genome of hyperthermophilic archaeon, Thermococcus kodakarensis". Extremophiles. 17 (1): 153–60. doi:10.1007/s00792-012-0504-6. PMID   23224520. S2CID   15924402.
  4. ↑ Tae-Yang Jung, Y.-S. K., Byoung-Ha Oh, and Euijeon Woo (2012). "Identification of a novel ligand binding site in phosphoserine phosphatase from the hyperthermophilic archaeon Thermococcus onnurineus." Wiley Periodicals: 11.
  5. 1 2 3 4 5 6 7 8 9 Zhang Y, Zhao Z, Chen CT, Tang K, Su J, Jiao N (2012). "Sulfur metabolizing microbes dominate microbial communities in Andesite-hosted shallow-sea hydrothermal systems". PLOS ONE. 7 (9): e44593. Bibcode:2012PLoSO...744593Z. doi: 10.1371/journal.pone.0044593 . PMC   3436782 . PMID   22970260.
  6. 1 2 Antoine E, Guezennec J, Meunier JR, Lesongeur F, Barbier G (1995). "Isolation and Characterization of Extremely Thermophilic Archaebacteria Related to the Genus Thermococcus from Deep-Sea Hydrothermal Guaymas Basin". Current Microbiology. 31 (3): 7. doi:10.1007/bf00293552. S2CID   25215530.
  7. 1 2 Amenábar MJ, Flores PA, Pugin B, Boehmwald FA, Blamey JM (2013). "Archaeal diversity from hydrothermal systems of Deception Island, Antarctica". Polar Biology. 36 (3): 373–380. doi:10.1007/s00300-012-1267-3. S2CID   11705986.
  8. 1 2 Kim BK, Lee SH, Kim SY, Jeong H, Kwon SK, Lee CH, et al. (July 2012). "Genome sequence of an oligohaline hyperthermophilic archaeon, Thermococcus zilligii AN1, isolated from a terrestrial geothermal freshwater spring". Journal of Bacteriology. 194 (14): 3765–6. doi:10.1128/jb.00655-12. PMC   3393502 . PMID   22740682.
  9. ↑ Krupovic M, Gonnet M, Hania WB, Forterre P, Erauso G (2013). "Insights into dynamics of mobile genetic elements in hyperthermophilic environments from five new Thermococcus plasmids". PLOS ONE. 8 (1): e49044. Bibcode:2013PLoSO...849044K. doi: 10.1371/journal.pone.0049044 . PMC   3543421 . PMID   23326305.
  10. ↑ Hetzer A, Morgan HW, McDonald IR, Daughney CJ (July 2007). "Microbial life in Champagne Pool, a geothermal spring in Waiotapu, New Zealand". Extremophiles. 11 (4): 605–14. doi:10.1007/s00792-007-0073-2. PMID   17426919. S2CID   24239907.
  11. ↑ Tori K, Ishino S, Kiyonari S, Tahara S, Ishino Y (2013). "A novel single-strand specific 3'-5' exonuclease found in the hyperthermophilic archaeon, Pyrococcus furiosus". PLOS ONE. 8 (3): e58497. Bibcode:2013PLoSO...858497T. doi: 10.1371/journal.pone.0058497 . PMC   3591345 . PMID   23505520.
  12. ↑ Cui Z, Wang Y, Pham BP, Ping F, Pan H, Cheong GW, et al. (July 2012). "High level expression and characterization of a thermostable lysophospholipase from Thermococcus kodakarensis KOD1". Extremophiles. 16 (4): 619–25. doi:10.1007/s00792-012-0461-0. PMID   22622648. S2CID   17109990.
  13. ↑ Uehara R, Tanaka S, Takano K, Koga Y, Kanaya S (November 2012). "Requirement of insertion sequence IS1 for thermal adaptation of Pro-Tk-subtilisin from hyperthermophilic archaeon". Extremophiles. 16 (6): 841–51. doi:10.1007/s00792-012-0479-3. PMID   22996828. S2CID   10924828.
  14. ↑ Čuboňováa L, Katano M, Kanai T, Atomi H, Reeve JN, Santangelo TJ (December 2012). "An archaeal histone is required for transformation of Thermococcus kodakarensis". Journal of Bacteriology. 194 (24): 6864–74. doi:10.1128/jb.01523-12. PMC   3510624 . PMID   23065975.
  15. ↑ Postec A, Lesongeur F, Pignet P, Ollivier B, Querellou J, Godfroy A (November 2007). "Continuous enrichment cultures: insights into prokaryotic diversity and metabolic interactions in deep-sea vent chimneys". Extremophiles. 11 (6): 747–57. doi:10.1007/s00792-007-0092-z. hdl: 20.500.11850/58941 . PMID   17576518. S2CID   24258675.
  16. ↑ Eberly JO, Ely RL (2008). "Thermotolerant hydrogenases: biological diversity, properties, and biotechnological applications". Critical Reviews in Microbiology. 34 (3–4): 117–30. doi:10.1080/10408410802240893. PMID   18728989. S2CID   86357193.
  17. 1 2 Schut GJ, Boyd ES, Peters JW, Adams MW (March 2013). "The modular respiratory complexes involved in hydrogen and sulfur metabolism by heterotrophic hyperthermophilic archaea and their evolutionary implications". FEMS Microbiology Reviews. 37 (2): 182–203. doi: 10.1111/j.1574-6976.2012.00346.x . PMID   22713092.
  18. 1 2 Yuusuke Tokooji, T. S., Shinsuke Fujiwara, Tadayuki Imanaka and Haruyuki Atomi (2013). "Genetic Examination of Initial Amino Acid Oxidation and Glutamate Catabolism in the Hyperthermophilic Archaeon Thermococcus kodakarensis." Journal of Bacteriology: 10.
  19. ↑ Atomi H, Tomita H, Ishibashi T, Yokooji Y, Imanaka T (February 2013). "CoA biosynthesis in archaea". Biochemical Society Transactions. 41 (1): 427–31. doi:10.1042/bst20120311. PMID   23356323.
  20. ↑ "The LTP" . Retrieved 20 November 2023.
  21. ↑ "LTP_all tree in newick format" . Retrieved 20 November 2023.
  22. ↑ "LTP_08_2023 Release Notes" (PDF). Retrieved 20 November 2023.
  23. ↑ "GTDB release 08-RS214". Genome Taxonomy Database . Retrieved 10 May 2023.
  24. ↑ "ar53_r214.sp_label". Genome Taxonomy Database . Retrieved 10 May 2023.
  25. ↑ "Taxon History". Genome Taxonomy Database . Retrieved 10 May 2023.
  26. 1 2 3 4 Ozawa Y, Siddiqui MA, Takahashi Y, Urushiyama A, Ohmori D, Yamakura F, et al. (July 2012). "Indolepyruvate ferredoxin oxidoreductase: An oxygen-sensitive iron-sulfur enzyme from the hyperthermophilic archaeon Thermococcus profundus". Journal of Bioscience and Bioengineering. 114 (1): 23–7. doi:10.1016/j.jbiosc.2012.02.014. PMID   22608551.
  27. 1 2 3 4 5 6 7 8 Davidova IA, Duncan KE, Perez-Ibarra BM, Suflita JM (July 2012). "Involvement of thermophilic archaea in the biocorrosion of oil pipelines". Environmental Microbiology. 14 (7): 1762–71. doi:10.1111/j.1462-2920.2012.02721.x. PMID   22429327.
  28. ↑ Brown AM, Hoopes SL, White RH, Sarisky CA (December 2011). "Purine biosynthesis in archaea: variations on a theme". Biology Direct. 6: 63. doi: 10.1186/1745-6150-6-63 . PMC   3261824 . PMID   22168471.
  29. ↑ Duffaud GD, d'Hennezel OB, Peek AS, Reysenbach AL, Kelly RM (March 1998). "Isolation and characterization of Thermococcus barossii, sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent flange formation". Systematic and Applied Microbiology. 21 (1): 40–9. doi:10.1016/s0723-2020(98)80007-6. PMID   9741109.
  30. ↑ Petrova T, Bezsudnova EY, Boyko KM, Mardanov AV, Polyakov KM, Volkov VV, et al. (December 2012). "ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain". Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 68 (Pt 12): 1440–7. doi:10.1107/s1744309112043394. PMC   3509962 . PMID   23192021.
  31. 1 2 3 Amend JP (2009). "A brief review of microbial geochemistry in the shallow-sea hydrothermal system of Vulcano Island (Italy)". Freiberg Online Geoscience. 22: 7.
  32. ↑ Hughes RC, Coates L, Blakeley MP, Tomanicek SJ, Langan P, Kovalevsky AY, et al. (December 2012). "Inorganic pyrophosphatase crystals from Thermococcus thioreducens for X-ray and neutron diffraction". Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 68 (Pt 12): 1482–7. doi:10.1107/S1744309112032447. PMC   3509969 . PMID   23192028.
  33. ↑ 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.
  34. ↑ Itoh T (2003). "Taxonomy of Nonmethanogenic Hyperthermophilic and Related Thermophilic Archaea". Journal of Bioscience and Bioengineering. 96 (3): 203–212. doi:10.1263/jbb.96.203. PMID   16233511.
  35. ↑ Kuba Y, Ishino S, Yamagami T, Tokuhara M, Kanai T, Fujikane R, et al. (November 2012). "Comparative analyses of the two proliferating cell nuclear antigens from the hyperthermophilic archaeon, Thermococcus kodakarensis". Genes to Cells. 17 (11): 923–37. doi: 10.1111/gtc.12007 . PMID   23078585. S2CID   25416025.
  36. ↑ Hakon Dahle, F. G., Marit Madsen, Nils-Kare Birkeland (2008). "Microbial community structure analysis of produced water from a high-temperature North Sea oil-field." Antonie van Leeuwenhoek 93: 13.
  37. ↑ Ppyun H, Kim I, Cho SS, Seo KJ, Yoon K, Kwon ST (December 2012). "Improved PCR performance using mutant Tpa-S DNA polymerases from the hyperthermophilic archaeon Thermococcus pacificus". Journal of Biotechnology. 164 (2): 363–70. doi:10.1016/j.jbiotec.2013.01.022. PMID   23395617.
  38. 1 2 3 4 5 6 7 8 9 Marguet E, Gaudin M, Gauliard E, Fourquaux I, le Blond du Plouy S, Matsui I, Forterre P (February 2013). "Membrane vesicles, nanopods and/or nanotubes produced by hyperthermophilic archaea of the genus Thermococcus". Biochemical Society Transactions. 41 (1): 436–42. doi:10.1042/bst20120293. PMID   23356325.
  39. 1 2 3 4 5 Gaudin M, Gauliard E, Schouten S, Houel-Renault L, Lenormand P, Marguet E, Forterre P (February 2013). "Hyperthermophilic archaea produce membrane vesicles that can transfer DNA". Environmental Microbiology Reports. 5 (1): 109–16. doi:10.1111/j.1758-2229.2012.00348.x. PMID   23757139.
  40. 1 2 3 4 5 Li Z, Kelman LM, Kelman Z (February 2013). "Thermococcus kodakarensis DNA replication". Biochemical Society Transactions. 41 (1): 332–8. doi:10.1042/bst20120303. PMID   23356307.
  41. 1 2 3 4 5 6 Hirata A, Hori Y, Koga Y, Okada J, Sakudo A, Ikuta K, et al. (February 2013). "Enzymatic activity of a subtilisin homolog, Tk-SP, from Thermococcus kodakarensis in detergents and its ability to degrade the abnormal prion protein". BMC Biotechnology. 13: 19. doi: 10.1186/1472-6750-13-19 . PMC   3599501 . PMID   23448268.
  42. 1 2 3 Trofimov AA, Slutskaya EA, Polyakov KM, Dorovatovskii PV, Gumerov VM, Popov VO (November 2012). "Influence of intermolecular contacts on the structure of recombinant prolidase from Thermococcus sibiricus". Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 68 (Pt 11): 1275–8. doi:10.1107/s174430911203761x. PMC   3515363 . PMID   23143231.
  43. ↑ Nisar MA, Rashid N, Bashir Q, Gardner QT, Shafiq MH, Akhtar M (July 2013). "TK1299, a highly thermostable NAD(P)H oxidase from Thermococcus kodakaraensis exhibiting higher enzymatic activity with NADPH". Journal of Bioscience and Bioengineering. 116 (1): 39–44. doi:10.1016/j.jbiosc.2013.01.020. PMID   23453203.

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