パイロコッカス・ホリコシイ
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/04/06 17:37:42」(JST)
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| Pyrococcus horikoshii |
| Scientific classification |
| Domain: |
Archaea |
| Kingdom: |
Euryarchaeota |
| Phylum: |
Euryarchaeota |
| Class: |
Thermococci |
| Order: |
Thermococcales |
| Family: |
Thermococcaceae |
| Genus: |
Pyrococcus |
| Species: |
P. horikoshii |
| Binomial name |
Pyrococcus horikoshii
Erauso et al. 1993 |
Pyrococcus horikoshii is a hyperthermophilic, anaerobic archaeon, first isolated from hydrothermal fluid samples obtained at the Okinawa Trough vents at a depth of 1,395 metres (4,577 ft). It is obligately heterotrophic, cells are irregular cocci with a tuft of flagella, growing optimally at 98 °C, sulphur greatly enhancing its growth.[1]
References
- ^ González, Juan M.; Masuchi, Yaeko; Robb, F. T.; Ammerman, James W.; et al. (1998). "Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough". Extremophiles 2 (2): 123–130. doi:10.1007/s007920050051. ISSN 1431-0651.
Further reading
- Theriot, Casey M.; Semcer, Rebecca L.; Shah, Saumil S.; Grunden, Amy M. (2011). "Improving the Catalytic Activity of Hyperthermophilic Pyrococcus horikoshii Prolidase for Detoxification of Organophosphorus Nerve Agents over a Broad Range of Temperatures". Archaea 2011: 1–9. doi:10.1155/2011/565127. ISSN 1472-3646.
- Ando, Susumu; Ishikawa, Kazuhiko; Ishida, Hiroyasu; Kawarabayasi, Yutaka; et al. (1999). "Thermostable aminopeptidase from Pyrococcus horikoshii". FEBS Letters 447 (1): 25–28. doi:10.1016/S0014-5793(99)00257-4. ISSN 0014-5793.
- Appolaire A; Rosenbaum E; Durá MA; et al. (August 2013). "Pyrococcus horikoshii TET2 Peptidase Assembling Process and Associated Functional Regulation". The Journal of Biological Chemistry 288 (31): 22542–54. doi:10.1074/jbc.M113.450189. PMID 23696647. Retrieved 2013-08-06.
- Ando S; Ishida H; Kosugi Y; Ishikawa K (January 2002). "Hyperthermostable endoglucanase from Pyrococcus horikoshii". Applied and Environmental Microbiology 68 (1): 430–3. doi:10.1128/AEM.68.1.430-433.2002. PMC 126571. PMID 11772658. Retrieved 2013-08-06.
- Manjunath K; Kanaujia SP; Kanagaraj S; Jeyakanthan J; et al. (February 2013). "Structure of SAICAR synthetase from Pyrococcus horikoshii OT3: insights into thermal stability". International Journal of Biological Macromolecules 53: 7–19. doi:10.1016/j.ijbiomac.2012.10.028. PMID 23137517. Retrieved 2013-08-06.
External links
- Pyrococcus horikoshii at the Encyclopedia of Life
- WORMS entry
- LPSN
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Extremophiles
|
|
| Types |
- Acidophile
- Alkaliphile
- Capnophile
- Cryozoa
- Endolith
- Halophile
- Hypolith
- Lipophile
- Lithoautotroph
- Lithophile
- Methanogen
- Metallotolerant
- Oligotroph
- Osmophile
- Piezophile
- Polyextremophile
- Psammophile
- Psychrophile
- Radioresistant
- Thermophile / Hyperthermophile
- Thermoacidophile
- Xerophile
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Notable
extremophiles |
|
Bacteria
|
- Chloroflexus aurantiacus
- Deinococcus radiodurans
- Deinococcus–Thermus
- Snottite
- Thermus aquaticus
- Thermus thermophilus
- Spirochaeta americana
- GFAJ-1
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|
|
Archaea
|
- Pyrococcus furiosus
- Strain 121
- Pyrolobus fumarii
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|
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Animalia
|
- Paralvinella sulfincola
- Halicephalobus mephisto
- Pompeii worm
- Tardigrada
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|
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| Related articles |
- Abiogenic petroleum origin
- Acidithiobacillales
- Acidobacteria
- Acidophiles in acid mine drainage
- Archaeoglobaceae
- Berkeley Pit
- Blood Falls
- Crenarchaeota
- Grylloblattidae
- Halobacteria
- Halobacterium
- Helaeomyia petrolei
- Hydrothermal vent
- Methanopyrus
- Movile Cave
- Radiotrophic fungus
- Rio Tinto
- Taq polymerase
- Thermostability
- Thermotogae
|
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UpToDate Contents
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English Journal
- Small-angle neutron scattering reveals the assembly mode and oligomeric architecture of TET, a large, dodecameric aminopeptidase.
- Appolaire A1, Girard E1, Colombo M1, Durá MA1, Moulin M2, Härtlein M2, Franzetti B1, Gabel F1.
- Acta crystallographica. Section D, Biological crystallography.Acta Crystallogr D Biol Crystallogr.2014 Nov;70(Pt 11):2983-93. doi: 10.1107/S1399004714018446. Epub 2014 Oct 23.
- The specific self-association of proteins into oligomeric complexes is a common phenomenon in biological systems to optimize and regulate their function. However, de novo structure determination of these important complexes is often very challenging for atomic-resolution techniques. Furthermore, in
- PMID 25372688
- The TET2 and TET3 aminopeptidases from Pyrococcus horikoshii form a hetero-subunit peptidasome with enhanced peptide destruction properties.
- Appolaire A1, Durá MA, Ferruit M, Andrieu JP, Godfroy A, Gribaldo S, Franzetti B.
- Molecular microbiology.Mol Microbiol.2014 Nov;94(4):803-14. doi: 10.1111/mmi.12775. Epub 2014 Oct 7.
- TET aminopeptidases assemble as large homo-dodecameric complexes. The reason why prokaryotic genomes often encode a diverse set of TET peptidases homologues remains unclear. In the archaeon Pyrococcus horikoshii, PhTET1, PhTET2 and PhTET3 homo-oligomeric particles have been proposed to work in conce
- PMID 25171083
- Thermodynamic analysis of unusually thermostable CutA1 protein from human brain and its protease susceptibility.
- Bagautdinov B1, Matsuura Y1, Yamamoto H1, Sawano M1, Ogasahara K2, Takehira M1, Kunishima N1, Katoh E3, Yutani K4.
- Journal of biochemistry.J Biochem.2014 Oct 24. pii: mvu062. [Epub ahead of print]
- Unusually stable proteins are a disadvantage for the metabolic turnover of proteins in cells. The CutA1 proteins from Pyrococcus horikoshii and from Oryza sativa (OsCutA1) have unusually high denaturation temperatures (Td) of nearly 150 and 100°C, respectively, at pH 7.0. It seemed that the CutA1 p
- PMID 25344844
Japanese Journal
- A Distinct Binding Mode of Archaeal Ribonuclease P Proteins to RNA
- ISHIHARA Masato,NISHIMOTO Etsuko,YAMASHITA Shoji [他]
- Bioscience, Biotechnology, and Biochemistry 76(12), 2335-2337, 2012-12-00
- NAID 40019531345
- Thermodynamic Analysis of a Multifunctional RNA-Binding Protein, PhoRpp38, in the Hyperthermophilic Archaeon Pyrococcus horikoshii OT3
- OSHIMA Kosuke,NAKASHIMA Takashi,KAKUTA Yoshimitsu [他],TSUMOTO Kouhei,KIMURA Makoto
- Bioscience, biotechnology, and biochemistry 76(6), 1252-1255, 2012-06-23
- … The protein component PhoRpp38 of Pyrococcus horikoshii ribonuclease P (RNase P) is known to be a multifunctional RNA-binding protein. …
- NAID 10030818671
- The Contribution of Peripheral Stem-Loops to the Catalytic Activity of Archaeal RNase P RNA from Pyrococcus horikoshii OT3
- Hara Tadashi,Terada Atsushi,Yamaguchi Hiroki [他],NAKASHIMA Takashi,KAKUTA Yoshimitsu,KIMURA Makoto
- Bioscience, biotechnology, and biochemistry 75(4), 816-819, 2011-04-23
- … We investigated the contribution of peripheral stem-loops to the catalytic activity of an archaeal RNase P RNA, <I>Pho</I>pRNA, from <I>Pyrococcus horikoshii</I> …
- NAID 10028272110
Related Links
- 嫌気性超好熱古細菌 (Pyrococcus horikoshii OT3 T (= NBRC 100139 T)) NBRC（旧ゲノム解析部門）で最初に解析の対象として選定したPyrococcus horikoshii OT3 T (= NBRC 100139 T)は、潜水艇「しんかい 2000」を用いた ...
- Classification: Higher Order Taxa Domain: Archaea; Phylum: Euryarchaeota; Class: Thermococci ; Order: Thermococcales ; Family: Thermococcaceae ; Genus: Pyrococcus (3). Species Pyrococcus horikoshii Description and ...
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