- 関
- acidophil、eosinophil、eosinophilic
WordNet
- a leukocyte readily stained with eosin (同)eosinophile
- of or relating to eosinophil
- archaebacteria that thrive in strongly acidic environments at high temperatures
- an organism that thrives in a relatively acid environment (同)acidophile
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/06/03 16:08:04」(JST)
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For other uses, see Acidophile (disambiguation).
Acidophiles or acidophilic organisms are those that thrive under highly acidic conditions (usually at pH 2.0 or below). These organisms can be found in different branches of the tree of life, including Archaea, Bacteria, and Eukaryotes.
Contents
- 1 List of acidophilic organisms
- 2 Mechanisms of adaptation to acidic environments
- 3 See also
- 4 References
- 5 Further reading
List of acidophilic organisms
A list of these organisms includes:
- Archaea
- Sulfolobales, an order in the Crenarchaeota branch[1] of Archaea
- Thermoplasmatales, an order in the Euryarchaeota branch[1] of Archaea
- ARMAN, in the Euryarchaeota branch[1] of Archaea
- Acidianus brierleyi, A. infernus, facultatively anaerobic thermoacidophilic archaebacteria
- Halarchaeum acidiphilum, acidophilic member of the Halobacteriacaeae[2]
- Metallosphaera sedula, thermoacidophilic
- Bacteria
- Acidobacterium,[3] a phylum of Bacteria
- Acidithiobacillales, an order of Proteobacteria e.g. A.ferrooxidans, A. thiooxidans
- Thiobacillus prosperus, T. acidophilus, T. organovorus, T. cuprinus
- Acetobacter aceti, a bacterium that produces acetic acid (vinegar) from the oxidation of ethanol.
- Alicyclobacillus, a genus of bacteria that can contaminate fruit juices.[4]
- Eukaryotes
- Mucor racemosus[5]
- Urotricha[5]
- Dunaliella acidophila[5]
- Philodina roseola[5]
Mechanisms of adaptation to acidic environments
Most acidophile organisms have evolved extremely efficient mechanisms to pump protons out of the intracellular space in order to keep the cytoplasm at or near neutral pH. Therefore, intracellular proteins do not need to develop acid stability through evolution. However, other acidophiles, such as Acetobacter aceti, have an acidified cytoplasm which forces nearly all proteins in the genome to evolve acid stability.[6] For this reason, Acetobacter aceti has become a valuable resource for understanding the mechanisms by which proteins can attain acid stability.
Studies of proteins adapted to low pH have revealed a few general mechanisms by which proteins can achieve acid stability. In most acid stable proteins (such as pepsin and the soxF protein from Sulfolobus acidocaldarius), there is an overabundance of acidic residues which minimizes low pH destabilization induced by a buildup of positive charge. Other mechanisms include minimization of solvent accessibility of acidic residues or binding of metal cofactors. In a specialized case of acid stability, the NAPase protein from Nocardiopsis alba was shown to have relocated acid-sensitive salt bridges away from regions that play an important role in the unfolding process. In this case of kinetic acid stability, protein longevity is accomplished across a wide range of pH, both acidic and basic.
See also
- Acidophiles in acid mine drainage
- Neutrophile
References
- ^ a b c http://141.150.157.117:8080/prokPUB/index.htm
- ^ Singh OV (2012). Extremophiles: Sustainable Resources and Biotechnological Implications. John Wiley & Sons. pp. 76–79. ISBN 978-1-118-10300-5.
- ^ Quaiser et al., Mol. Micro. 50, p.563.[full citation needed]
- ^ Pettipher GL, Osmundson ME, Murphy JM (March 1997). "Methods for the detection and enumeration of Alicyclobacillus acidoterrestris and investigation of growth and production of taint in fruit juice and fruit juice-containing drinks". Letters in Applied Microbiology 24 (3): 185–189. doi:10.1046/j.1472-765X.1997.00373.x. PMID 9080697.
- ^ a b c d Rawlings, Douglas; Johnson, D. Barrie. "Eukaryotic Acidophiles". Encyclopedia of Life Support System (EOLSS). Eolss Publishers. Retrieved 3 February 2014.
- ^ Menzel, U.; Gottschalk, G. (1985). "The internal pH of Acetobacterium wieringae and Acetobacter aceti during growth and production of acetic acid". Arch Microbiol 143 (1): 47–51. doi:10.1007/BF00414767.
Further reading
- Cooper, J. B.; Khan, G.; Taylor, G.; Tickle, I. J.; Blundell, T. L. (July 1990). "X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution". J Mol Biol 214 (1): 199–222. doi:10.1016/0022-2836(90)90156-G. PMID 2115088.
- Bonisch, H.,; Schmidt, C. L.; Schafer, G.; Ladenstein, R. (June 2002). "The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 A resolution". J Mol Biol 319 (3): 791–805. doi:10.1016/S0022-2836(02)00323-6. PMID 12054871.
- Schafer, K; Magnusson, U; Scheffel, F; Schiefner, A; Sandgren, MO; Diederichs, K; Welte, W; Hülsmann, A; Schneider, E; Mowbray, SL (January 2004). "X-ray structures of the maltose-maltodextrin-binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins". Journal of Molecular Biology 335 (1): 261–74. doi:10.1016/j.jmb.2003.10.042. PMID 14659755.
- Walter, R. L.; Ealick, S. E.; Friedman, A. M.; Blake, R. C. 2nd; Proctor, P.; Shoham, M. (November 1996). "Multiple wavelength anomalous diffraction (MAD) crystal structure of rusticyanin: a highly oxidizing cupredoxin with extreme acid stability". J Mol Biol 263 (5): 730–51. doi:10.1006/jmbi.1996.0612. PMID 8947572.
- Botuyan, M. V.; Toy-Palmer, A.; Chung, J.; Blake, R. C. 2nd; Beroza, P.; Case, D. A.; Dyson, H. J. (1996). "NMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: structural basis for the extreme acid stability and redox potential". J Mol Biol 263 (5): 752–67. doi:10.1006/jmbi.1996.0613. PMID 8947573.
- Kelch, B. A.; Eagen, K. P.; Erciyas, F. P.; Humphris, E. L.; Thomason, A. R.; Mitsuiki, S.; Agard, D. A. (May 2007). "Structural and mechanistic exploration of acid resistance: kinetic stability facilitates evolution of extremophilic behavior". J Mol Biol 368 (3): 870–883. doi:10.1016/j.jmb.2007.02.032. PMID 17382344.
Extremophiles
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Types |
- Acidophile
- Alkaliphile
- Capnophile
- Cryozoa
- Endolith
- Halophile
- Hypolith
- Lipophile
- Lithoautotroph
- Lithophile
- Methanogen
- Metallotolerant
- Oligotroph
- Osmophile
- Piezophile
- Polyextremophile
- 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
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- Pyrococcus furiosus
- Strain 121
- Pyrolobus fumarii
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Animalia
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- Paralvinella sulfincola
- Halicephalobus mephisto
- Pompeii worm
- Tardigrada
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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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English Journal
- Lipase production from a novel thermo-tolerant and extreme acidophile Bacillus pumilus using palm oil as the substrate and treatment of palm oil-containing wastewater.
- Saranya P1, Sukanya Kumari H, Prasad Rao B, Sekaran G.
- Environmental science and pollution research international.Environ Sci Pollut Res Int.2014 Mar;21(5):3907-19. doi: 10.1007/s11356-013-2354-x. Epub 2013 Nov 29.
- The thermo-tolerant and extreme acidophilic microorganism Bacillus pumilus was isolated from the soil collected from a commercial edible-oil extraction industry. Optimisation of conditions for the lipase production was conducted using response surface methodology. The optimum conditions for obtainin
- PMID 24293300
- α-fur, an antisense RNA gene to fur in the extreme acidophile Acidithiobacillus ferrooxidans.
- Lefimil C1, Jedlicki E, Holmes DS.
- Microbiology (Reading, England).Microbiology.2014 Mar;160(Pt 3):514-24. doi: 10.1099/mic.0.073171-0. Epub 2014 Jan 2.
- A large non-coding RNA, termed α-Fur, of ~1000 nt has been detected in the extreme acidophile Acidithiobacillus ferrooxidans encoded on the antisense strand to the iron-responsive master regulator fur (ferric uptake regulator) gene. A promoter for α-fur was predicted bioinformatically and validate
- PMID 24385477
- New copper resistance determinants in the extremophile acidithiobacillus ferrooxidans: a quantitative proteomic analysis.
- Almárcegui RJ1, Navarro CA, Paradela A, Albar JP, von Bernath D, Jerez CA.
- Journal of proteome research.J Proteome Res.2014 Feb 7;13(2):946-60. doi: 10.1021/pr4009833. Epub 2014 Jan 8.
- Acidithiobacillus ferrooxidans is an extremophilic bacterium used in biomining processes to recover metals. The presence in A. ferrooxidans ATCC 23270 of canonical copper resistance determinants does not entirely explain the extremely high copper concentrations this microorganism is able to stand, s
- PMID 24380576
Japanese Journal
- 2Ca15 Acidithiobacillus ferrooxidansの新規なチオ硫酸デヒドロゲナーゼの性質(酵素学,酵素工学,一般講演)
- Optimization of medium components and cultural variables for enhanced production of acidic high maltose-forming and Ca^<2+> -independent α-amylase by Bacillus acidicola(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- A new acidophilic fungus Teratosphaeria acidotherma (Capnodiales, Ascomycota) from a hot spring
Related Links
- Acidophiles or Acidophilic organisms are those that thrive under highly acidic conditions (usually at pH 2.0 or below). These organisms can be found in different branches of the tree of life, including Archaea, Bacteria, and Eukaryotes.
- 27 Jul 2008 ... Acidophiles are organisms that can withstand and even thrive in acidic environments where the pH values range from ... Acidophiles include certain types of eukaryotes, bacteria and archaea that are found in a variety of acidic ...
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- 関
- acidophil、acidophile、acidophilic、eosinophil