Difference between revisions of "Pyrococcus furiosus"

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| species = ''P. furiosus''
 
| species = ''P. furiosus''
 
| binomial = ''Pyrococcus furiosus''
 
| binomial = ''Pyrococcus furiosus''
| binomial_authority = Erauso et al. 1993
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| binomial_authority = Erauso ''et al.'' 1993
 
}}
 
}}
'''''Pyrococcus furiosus''''' is a heat-requiring [[extremophile]] species of [[Archaea]], ([[procaryote]]s with a different ancestry than ordinary bacteria--and possibly everything else).   It is one of the few organisms identified as possessing enzymes containing [[tungsten]], an element rarely found in biological molecules.
+
'''''Pyrococcus furiosus''''' is a heat-requiring [[extremophile]] species of [[Archaea]], ([[procaryote]]s with a different ancestry than ordinary bacteria--and possibly everything else). It is one of the few organisms that has enzymes which contain [[tungsten]], an element rarely found in biological molecules.
 
+
The name ''Pyrococcus'' meaning 'fireball' in Latin, refers to the extremophile's round shape and its ability to grow in temperatures of around 100 degrees Celsius. The species name ''furiosus'' means 'rushing', and refers to the extremophile's doubling time.
  
 
==Properties==
 
==Properties==
''Pyrococcus furiosus'' is noted for its rapid doubling time of 37 minutes under its unusual optimal conditions.
+
''Pyrococcus furiosus'' is noted for its rapid rate of reproduction (its doubling time is 37 minutes under its unusual optimal conditions). It appears as mostly regular cocci of 0.8 µm to 1.5 µm diameter with
It appears as mostly regular cocci of 0.8 µm to 1.5 µm diameter with
+
 
monopolar polytrichous flagellation. It grows between 70 ºC and 103 ºC,
 
monopolar polytrichous flagellation. It grows between 70 ºC and 103 ºC,
 
with an optimum temperature of 100 ºC, and between pH 5 and 9 (with an optimum at
 
with an optimum temperature of 100 ºC, and between pH 5 and 9 (with an optimum at
pH 7). It grows well on yeast extract, [[maltose]], [[cellobiose]], ß-glucans, [[starch]], and protein
+
pH 7). It grows well on yeast extract, [[maltose]], [[cellobiose]], ß-glucans, [[starch]], and protein sources (tryptone, peptone, casein and meat extracts). Growth is very slow, or nonexistent, on amino acids, organic acids, alcohols, and most carbohydrates (including [[glucose]], [[fructose]], [[lactose]] and [[galactose]]).
sources (tryptone, peptone, casein and meat extracts). Growth is very slow, or nonexistent,
+
on amino acids, organic acids, alcohols, and most carbohydrates (including
+
[[glucose]], [[fructose]], [[lactose]] and [[galactose]]).
+
  
 
The ability to grow on polysaccharides (maltose, cellobiose, starch) but not on
 
The ability to grow on polysaccharides (maltose, cellobiose, starch) but not on
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''Pyrococcus furiosus'' has an unusual [[glycolysis|glycolytic]] pathway: its [[hexokinase]] and [[phosphofructokinase]] hydrolize [[ADP]], instead of [[ATP]]. Moreover, although it contains a [[glyceraldehyde-3-phosphate dehydrogenase]], this enzyme is repressed during glycolysis. Glyceraldehyde-3-P oxidation to glycerate-3-P is instead performed in a single step (without ATP formation) by a tungsten-containing glyceraldehyde-3-P:ferredoxin oxidoreductase. Electrons released in glycolysis are transferred by a [4Fe-4S] ferredoxin to a membrane-bound [[hydrogenase]], which reduces H<sup>+</sup> to H<sub>2</sub>, and uses the released energy to create a proton gradient, which enables ATP synthesis through an ATP synthetase.  
 
''Pyrococcus furiosus'' has an unusual [[glycolysis|glycolytic]] pathway: its [[hexokinase]] and [[phosphofructokinase]] hydrolize [[ADP]], instead of [[ATP]]. Moreover, although it contains a [[glyceraldehyde-3-phosphate dehydrogenase]], this enzyme is repressed during glycolysis. Glyceraldehyde-3-P oxidation to glycerate-3-P is instead performed in a single step (without ATP formation) by a tungsten-containing glyceraldehyde-3-P:ferredoxin oxidoreductase. Electrons released in glycolysis are transferred by a [4Fe-4S] ferredoxin to a membrane-bound [[hydrogenase]], which reduces H<sup>+</sup> to H<sub>2</sub>, and uses the released energy to create a proton gradient, which enables ATP synthesis through an ATP synthetase.  
 
 
  
 
==Discovery==
 
==Discovery==
''Pyrococcus furiosus'' was originally isolated [[Anaerobic organism|anaerobically]] from geothermally heated marine sediments with temperatures between 90 ºC and 100 ºC collected at the beach of Porto Levante, [[Vulcano Island]], Italy. It was first described by Dr [[Karl Stetter]] of the [[University of Regensburg]] in Germany, and a colleague, Dr Gerhard Fiala.
+
''Pyrococcus furiosus'' was originally isolated [[Anaerobic organism|anaerobically]] from geothermally heated marine sediments with temperatures between 90 ºC and 100 ºC collected at the beach of Porto Levante, Vulcano Island, Italy. It was first described by Dr Karl Stetter of the University of Regensburg in Germany, and a colleague, Dr Gerhard Fiala.
  
 
==Genome==
 
==Genome==
The sequencing of the complete [[genome]] of ''Pyrococcus furiosus'' was completed in 2001 by scientists at the [[University of Maryland Biotechnology Institute]] The Maryland team found that the genome had 1,908 kilobases, coding for some 2,065 proteins.
+
The sequencing of the complete [[genome]] of ''Pyrococcus furiosus'' was completed in 2001 at the [[University of Maryland Biotechnology Institute]] The Maryland team found that the genome had 1,908 kilobases, coding for 2,065 proteins.
 
+
==The extremophile's scientific name==
+
The name ''Pyrococcus'' means 'fireball' in Latin, to refer to the extremophile's round shape and ability to grow in temperatures of around 100 degrees Celsius. The species name ''furiosus'' means 'rushing', and refers to the extremophile's doubling time.
+
  
 
==Uses==
 
==Uses==
The [[enzymes]] of ''Pyrococcus furiosus'' as would obviously be expected, are extremely thermostable. Consequently [[DNA Polymerase]] from ''Pyrococcus furiosus'', are often used in the [[Polymerase Chain Reaction]], with the relevant enzyme known as [[Pfu]]. At temperatures where other interfering enzymes are destroyed, the activity of this enzyme remains.   
+
The [[enzymes]] of ''Pyrococcus furiosus'' as would be expected, are extremely thermostable. Consequently [[DNA Polymerase]] from ''Pyrococcus furiosus'', are often used in the [[Polymerase Chain Reaction]], with the relevant enzyme known as [[Pfu]]. At temperatures where other interfering enzymes are destroyed, the activity of this enzyme remains.   
  
 
==References==
 
==References==
 
*{{cite journal
 
*{{cite journal
| author = Fiala G. and Stetter K.O.
+
| author = Fiala G, Stetter KO
 
| year = 1986
 
| year = 1986
 
| title = ''Pyrococcus furiosus'' sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C
 
| title = ''Pyrococcus furiosus'' sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C
Line 58: Line 49:
 
}}
 
}}
 
*{{cite journal
 
*{{cite journal
| author = Robb F.T., Maeder D.L., Brown J.R., DiRuggiero J., Stump M.D., Yeh R.K., Weiss R.B., Dunn D.M.
+
| author = Robb FT ''et al.''
 
| year = 2001
 
| year = 2001
 
| title = Genomic sequence of hyperthermophile, ''Pyrococcus furiosus'': implications for physiology and enzymology
 
| title = Genomic sequence of hyperthermophile, ''Pyrococcus furiosus'': implications for physiology and enzymology
Line 65: Line 56:
 
| pages = 134&ndash;57
 
| pages = 134&ndash;57
 
}}
 
}}
* van der Oost J, Schut G, Kengen SW, Hagen WR, Thomm M, de Vos WM. (1998)The Ferredoxin-dependent Conversion of Glyceraldehyde-3-phosphate in the Hyperthermophilic Archaeon Pyrococcus furiosus Represents a Novel Site of Glycolytic Regulation [http://www.jbc.org/cgi/reprint/273/43/28149 J Biol Chem. 273:28149-28154]
+
* van der Oost J ''et al.''(1998)The Ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon ''pyrococcus furiosus'' represents a novel Site of glycolytic regulation [http://www.jbc.org/cgi/reprint/273/43/28149 ''J Biol Chem'' 273:28149-54]
* Silva PJ, van den Ban EC, Wassink H, Haaker H, de Castro B, Robb FT, Hagen WR. (2000) Enzymes of hydrogen metabolism in Pyrococcus furiosus. [http://dx.doi.org/10.1046/j.1432-1327.2000.01745.x Eur. J. Bioch., 267: 6541-6550 ]
+
* Silva PJ ''et al.'' (2000) Enzymes of hydrogen metabolism in Pyrococcus furiosus. [http://dx.doi.org/10.1046/j.1432-1327.2000.01745.x ''Eur J Bioch'', 267: 6541-50 ]
* Rajat Sapra, Karine Bagramyan, and Michael W. W. Adams (2003) A simple energy-conserving system: Proton reduction coupled to proton translocation. [http://dx.doi.org/10.1073/pnas.1331436100 Proc. Natl. Acad. Sci. USA, 100, 7545-7550]
+
* Sapra R ''et al.''(2003) A simple energy-conserving system: Proton reduction coupled to proton translocation. [http://dx.doi.org/10.1073/pnas.1331436100 ''Proc Natl Acad Sci USA'' 100:7545-50]

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Pyrococcus furiosus
Scientific classification
Kingdom: Archaea
Phylum: Euryarchaeota
Class: Thermococci
Order: Thermococcales
Family: Thermococcaceae
Genus: Pyrococcus
Species: P. furiosus
Binomial name
Pyrococcus furiosus
Erauso et al. 1993

Pyrococcus furiosus is a heat-requiring extremophile species of Archaea, (procaryotes with a different ancestry than ordinary bacteria--and possibly everything else). It is one of the few organisms that has enzymes which contain tungsten, an element rarely found in biological molecules. The name Pyrococcus meaning 'fireball' in Latin, refers to the extremophile's round shape and its ability to grow in temperatures of around 100 degrees Celsius. The species name furiosus means 'rushing', and refers to the extremophile's doubling time.

Properties

Pyrococcus furiosus is noted for its rapid rate of reproduction (its doubling time is 37 minutes under its unusual optimal conditions). It appears as mostly regular cocci of 0.8 µm to 1.5 µm diameter with monopolar polytrichous flagellation. It grows between 70 ºC and 103 ºC, with an optimum temperature of 100 ºC, and between pH 5 and 9 (with an optimum at pH 7). It grows well on yeast extract, maltose, cellobiose, ß-glucans, starch, and protein sources (tryptone, peptone, casein and meat extracts). Growth is very slow, or nonexistent, on amino acids, organic acids, alcohols, and most carbohydrates (including glucose, fructose, lactose and galactose).

The ability to grow on polysaccharides (maltose, cellobiose, starch) but not on the monomeric sugars suggests that oligosaccharides with various degrees of polymerization may be imported into the cell, and only afterwards hydrolyzed to glucose.

Pyrococcus furiosus has an unusual glycolytic pathway: its hexokinase and phosphofructokinase hydrolize ADP, instead of ATP. Moreover, although it contains a glyceraldehyde-3-phosphate dehydrogenase, this enzyme is repressed during glycolysis. Glyceraldehyde-3-P oxidation to glycerate-3-P is instead performed in a single step (without ATP formation) by a tungsten-containing glyceraldehyde-3-P:ferredoxin oxidoreductase. Electrons released in glycolysis are transferred by a [4Fe-4S] ferredoxin to a membrane-bound hydrogenase, which reduces H+ to H2, and uses the released energy to create a proton gradient, which enables ATP synthesis through an ATP synthetase.

Discovery

Pyrococcus furiosus was originally isolated anaerobically from geothermally heated marine sediments with temperatures between 90 ºC and 100 ºC collected at the beach of Porto Levante, Vulcano Island, Italy. It was first described by Dr Karl Stetter of the University of Regensburg in Germany, and a colleague, Dr Gerhard Fiala.

Genome

The sequencing of the complete genome of Pyrococcus furiosus was completed in 2001 at the University of Maryland Biotechnology Institute The Maryland team found that the genome had 1,908 kilobases, coding for 2,065 proteins.

Uses

The enzymes of Pyrococcus furiosus as would be expected, are extremely thermostable. Consequently DNA Polymerase from Pyrococcus furiosus, are often used in the Polymerase Chain Reaction, with the relevant enzyme known as Pfu. At temperatures where other interfering enzymes are destroyed, the activity of this enzyme remains.

References

  • Fiala G, Stetter KO (1986). "Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C". Archives of Microbiology 145: 56–61.
  • Robb FT et al. (2001). "Genomic sequence of hyperthermophile, Pyrococcus furiosus: implications for physiology and enzymology". Methods in Enzymology 330: 134–57.
  • van der Oost J et al.(1998)The Ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon pyrococcus furiosus represents a novel Site of glycolytic regulation J Biol Chem 273:28149-54
  • Silva PJ et al. (2000) Enzymes of hydrogen metabolism in Pyrococcus furiosus. Eur J Bioch, 267: 6541-50
  • Sapra R et al.(2003) A simple energy-conserving system: Proton reduction coupled to proton translocation. Proc Natl Acad Sci USA 100:7545-50