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- メタノカルドコックス・ヤンナスキイ
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/12/26 05:23:35」(JST)
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Methanocaldococcus jannaschii |
Scientific classification |
Domain: |
Archaea |
Kingdom: |
Euryarchaeota |
Phylum: |
Euryarchaeota |
Class: |
Methanococci |
Order: |
Methanococcales |
Family: |
Methanocaldococcaceae |
Genus: |
Methanocaldococcus |
Species: |
Methanocaldococcus jannaschii |
Synonyms |
- Methanococcus jannaschii (Jones 1983)
|
Methanocaldococcus jannaschii (formerly Methanococcus jannas chii) is a thermophilic methanogenic archaea in the class Methanococci. It was the first archaeon to have its complete genome sequenced.[1] The sequencing identified many genes unique to the archaea. Many of the synthesis pathways for methanogenic cofactors were worked out biochemically in this organism,[2] as were several other archaeal-specific metabolic pathways.
Contents
- 1 History
- 2 Sequencing
- 3 Taxonomy
- 4 Biology and biochemistry
- 5 References
- 6 Further reading
- 7 External links
History
Methanocaldococcus jannaschii was isolated from a submarine hydrothermal vent at Woods Hole Oceanographic Institution.[3]
Sequencing
Methanocaldococcus jannaschii was sequenced by a group at TIGR led by Craig Venter[4] using whole genome shotgun sequencing. M. jannaschii represented the first member of the Archaea to have its genome sequenced. According to Venter, the unique features of the genome provided strong evidence that there are three domains of life.[5]
Taxonomy
Methanocaldoccus jannaschii is a member of the genus Methanocaldococcus (previously a part of Methanococcus) and is therefore sometimes referred to as a "class I" methanogen (e.g. [1]).
Biology and biochemistry
M. jannaschii is a thermophilic methanogen, meaning it grows by making methane as a metabolic byproduct. It is only capable of growth on carbon dioxide and hydrogen as primary energy sources, unlike many other methanococci (such as Methanococcus maripalidus) which can also use formate as a primary energy source.[6] The genome includes many hydrogenases, such as a 5,10-methenyltetrahydromethanopterin hydrogenase,[7] a ferredoxin hydrogenase (eha), and a Coenzyme F420 hydrogenase.[8]
Proteomic studies showed that M. jannaschii contains a large number of inteins: 19 were discovered by one study.[9]
Many novel metabolic pathways have been worked out in M. jannaschii, including the pathways for synthesis of many methanogenic cofactors,[10] riboflavin,[11] and novel amino acid synthesis pathways .[citation needed] Many information processing pathways have also been studied in this organism, such as an archaeal-specific DNA polymerase family.[12]
References
- ^ Bult CJ, et al. (1996). "Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii.". Science 273 (5278): 1058–1073. doi:10.1126/science.273.5278.1058. PMID 8688087.
- ^ White R. (2001). "Biosynthesis of the methanogenic cofactors.". Vitamins and Hormones 61: 299–337. doi:10.1016/s0083-6729(01)61010-0. PMID 11153270.
- ^ Jones WJ, et al. (1983). "Methanococcus jannaschii sp. nov., an extremely thermophilic methanogen from a submarine hydrothermal vent". Arch. Microbiol. 136 (4): 254–261. doi:10.1007/BF00425213.
- ^ Wade N. (23 August 1996). "Deep Sea Yields a Clue to Life's Origin.". New York Times.
- ^ Wade N. et al. ibid.
- ^ Jones et al. ibid.
- ^ Lyon EJ, Shima S, Buurman G, Chowdhuri S, Batschauer A, Steinbach K, Thauer RK (January 2004). "UV-A/blue-light inactivation of the 'metal-free' hydrogenase (Hmd) from methanogenic archaea". Eur. J. Biochem. 271 (1): 195–204. doi:10.1046/j.1432-1033.2003.03920.x. PMID 14686932.
- ^ Thauer; et al. (2010). "Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H2 Storage". Ann. Rev. Biochem. 79: 507–536. doi:10.1146/annurev.biochem.030508.152103.
- ^ Zhu W, et al. (2004). "Shotgun Proteomics of Methanococcus jannaschii and Insights into Methanogenesis". J. Proteome Res. 3 (3): 538–548. doi:10.1021/pr034109s. PMID 15253435. .
- ^ White R. Ibid.
- ^ Haase I, Mörtl S, Köhler P, Bacher A, Fischer M. (2003). "Biosynthesis of riboflavin in archaea. 6,7-dimethyl-8-ribityllumazine synthase of Methanococcus jannaschii". Eur J Biochem. 270 (5): 1025–1032. doi:10.1046/j.1432-1033.2003.03478.x. PMID 12603336.
- ^ Ishino Y, et al. "A Novel DNA Polymerase Family Found in Archaea". J. bacteriol. 180 (8): 2232–2236.
Further reading
- Gao, yongxiang (November 2013). "Crystallization and preliminary X-ray diffraction analysis of MJ0458, an adenylate kinase from Methanocaldococcus jannaschii". Acta Crystallographica Section F Structural Biology and Crystallization Communications: 1272-1274. doi:10.1107/S1744309113026638. PMID 24192367.
- Wang, Yu; Xu, Huimin; White, Robert H. (August 2014). "Beta-Alanine Biosynthesis in Methanocaldococcus jannaschii". American Society for Microbiology 196: 2869–2875. doi:10.1128/JB.01784-14.
- Allen, Kyle D.; Xu, Huimin; White, Robert H. (September 2014). "Identification of a Unique Radical S-Adenosylmethionine Methylase Likely Involved in Methanopterin Biosynthesis in Methanocaldococcus jannaschii". Journal of Bacteriology 196 (18): 3315–3323. doi:10.1128/JB.01903-14.
- Lee, Eun Hye; Lee, Kitaik; Hwang, Kwang Yeon (13 December 2013). "Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii" 70 (Pt 4): 922-931. doi:10.1107/S1399004713033762.
External links
- Microbe wiki entry for Methano(caldo)coccus jannaschii
- UCSD genome browser entry for Methanocaldococcus jannaschii
- KEGG entry for Methanocaldococcus jannaschii
English Journal
- The Cryo-EM structure of the CorA channel from Methanocaldococcus jannaschii in low magnesium conditions.
- Cleverley RM1, Kean J1, Shintre CA1, Baldock C1, Derrick JP1, Ford RC1, Prince SM2.
- Biochimica et biophysica acta.Biochim Biophys Acta.2015 Oct;1848(10 Pt A):2206-15. doi: 10.1016/j.bbamem.2015.06.002. Epub 2015 Jun 4.
- CorA channels are responsible for the uptake of essential magnesium ions by bacteria. X-ray crystal structures have been resolved for two full-length CorA channels, each in a non-conducting state with magnesium ions bound to the protein: These structures reveal a homo-pentameric quaternary structure
- PMID 26051127
- Optimisation of a system for the co-translational incorporation of a keto amino acid and its application to a tumour-specific Anticalin.
- Reichert AJ1, Poxleitner G1, Dauner M1, Skerra A2.
- Protein engineering, design & selection : PEDS.Protein Eng Des Sel.2015 Sep 23. pii: gzv048. [Epub ahead of print]
- The bioorthogonal keto group has attracted interest for the site-specific chemical conjugation of recombinant proteins under mild conditions, e.g. with aminooxy-functionalised fluorescent probes, radiometal chelates, toxins or polymers. However, the cotranslational incorporation of the corresponding
- PMID 26405058
- Towards a functional identification of catalytically inactive [Fe]-hydrogenase paralogs.
- Fujishiro T1, Ataka K2, Ermler U3, Shima S1,4.
- The FEBS journal.FEBS J.2015 Sep;282(17):3412-23. doi: 10.1111/febs.13351. Epub 2015 Jul 14.
- [Fe]-hydrogenase (Hmd), an enzyme of the methanogenic energy metabolism, harbors an iron-guanylylpyridinol (FeGP) cofactor used for H2 cleavage. The generated hydride is transferred to methenyl-tetrahydromethanopterin (methenyl-H4 MPT(+) ). Most hydrogenotrophic methanogens contain the hmd-related g
- PMID 26094576
Japanese Journal
- Analyses of Conditions for KMSSS Loop in Tyrosyl-tRNA Synthetase by Building a Mutant Library
- 藤井 秋彦,若林 健一,小野寺 賢司 [他],KAMIJO Shunsuke
- 生産研究 60(6), 583-589, 2008
- … For that purpose, we build a library of more than two hundred mutants substituting the KMSSS loop, Lys204-Met205-Ser206-Ser207-Ser208, in tyrosyl-tRNA synthetase of Methanococcus jannaschii, and their degrees of catalytic were examined by the Amber suppression method. …
- NAID 130000102320
- Nucleotide composition of the genomic and protein-coding sequences in the two DNA strands
- Nakashima Hiroshi
- IFMBE Proceedings 21(1), 867-870, 2008
- … The nucleotide composition of protein-coding genes in the two DNA strands of Escherichia coli, Bacillus subtilis, Methanococcus jannaschii and mitochondrial genes of human and fruit fly was studied. … jannaschii indicated compositional asymmetry in their genomic sequences. … jannaschii. …
- NAID 120002647976
- 1E15-1 Methanococcus jannaschii由来新規NADPフォスファターゼ/NADキナーゼ融合タンパク質MJ0917の機能解析(生物化学工学,一般講演)
Related Links
- Methanococcus jannaschii belongs to a specific group called methanogens, or methane producers (Tumbula and Whitman, 1999). Methanogens are physiologically specialized to undergo fueling reactions to produce methane as the ...
- Description and Significance M. jannaschii was the first Archaeon to have its genome sequenced, which opened the doors for comparison between the genomes of the three domains. It was originally located from a sediment sample ...
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