Isolation, taxonomy and phylogeny of hyperthermophilic microorganisms

Blöchl, E.; Burggraf, Siegfried; Fiala, Gerhard; Lauerer, Gerta; Huber, Gertrud; Huber, Robert; Rachel, Reinhard; Segerer, Andreas H.; Stetter, Karl O.; Völkl, Paul

doi:10.1007/bf00339133

Cited by 78 publications

(28 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These organisms belong to the Bacteria and to the Archaea , although the latter domain includes a larger variety of organisms living at higher temperatures than the former. The term thermophile is often used to define organisms that have optimum growth temperatures between 65 ° C and 80 ° C, while hyperthermophilic organisms are those with optimum growth temperatures above 80 ° C. (Blöchl et al ., 1995).…”

mentioning

confidence: 99%

“…On the other hand, hyperthermophilic organisms, with a few notable exceptions such as the species of the Order Sulfolobales , Pyrobaculum islandicum and Thermococcus zilligii , originate from shallow or abyssal marine geothermal areas (Blöchl et al ., 1995). The water in shallow marine or abyssal environments is generally saline but, varies from low salinity to that of seawater.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Compatible solutes of organisms that live in hot saline environments

Santos

Costa

2002

Environmental Microbiology

249

206

View full text Add to dashboard Cite

SummaryThe accumulation of organic solutes is a prerequisite for osmotic adjustment of all microorganisms. Thermophilic and hyperthermophilic organisms generally accumulate very unusual compatible solutes namely, di-myo -inositol-phosphate, di-mannosyl-di-myoinositol-phosphate, di-glycerol-phosphate, mannosylglycerate and mannosylglyceramide, which have not been identified in bacteria or archaea that grow at low and moderate temperatures. There is also a growing awareness that some of these compatible solutes may have a role in the protection of cell components against thermal denaturation. Mannosylglycerate and di-glycerol-phosphate have been shown to protect enzymes and proteins from thermal denaturation in vitro as well, or better, than compatible solutes from mesophiles. The pathways leading to the synthesis of some of these compatible solutes from thermophiles and hyperthermophiles have been elucidated. However, large numbers of questions remain unanswered. Fundamental and applied interest in compatible solutes and osmotic adjustment in these organisms, drives research that, will, in the near future, allow us to understand the role of compatible solutes in osmotic protection and thermoprotection of some of the most fascinating organisms known on Earth.

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

Compatible solutes of organisms that live in hot saline environments

Santos

Costa

2002

Environmental Microbiology

249

206

View full text Add to dashboard Cite

show abstract

“…Pyrococcus furiosus is one of the best studied of an unusual group of microorganisms, the so-called hyperthermophilic archaea (formerly archaebacteria), which thrive at extreme temperatures and inhabit shallow and deep sea volcanic environments (1,2). P. furiosus grows optimally at 100°C and ferments either peptides or carbohydrates with the production of organic acids, H 2 and CO 2 .…”

mentioning

confidence: 99%

Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus , functions as a CoA-dependent pyruvate decarboxylase

Hutchins

Sung

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

118

116

View full text Add to dashboard Cite

Pyruvate ferredoxin oxidoreductase (POR) has been previously purified from the hyperthermophilic archaeon, Pyrococcus furiosus, an organism that grows optimally at 100°C by fermenting carbohydrates and peptides. The enzyme contains thiamine pyrophosphate and catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and CO 2 and reduces P. furiosus ferredoxin. Here we show that this enzyme also catalyzes the formation of acetaldehyde from pyruvate in a CoA-dependent reaction. Desulfocoenzyme A substituted for CoA showing that the cofactor plays a structural rather than a catalytic role. Ferredoxin was not necessary for the pyruvate decarboxylase activity of POR, nor did it inhibit acetaldehyde production. The apparent K m values for CoA and pyruvate were 0.11 mM and 1.1 mM, respectively, and the optimal temperature for acetaldehyde formation was above 90°C. These data are comparable to those previously determined for the pyruvate oxidation reaction of POR. At 80°C (pH 8.0), the apparent V m value for pyruvate decarboxylation was about 40% of the apparent V m value for pyruvate oxidation rate (using P. furiosus ferredoxin as the electron acceptor). Tentative catalytic mechanisms for these two reactions are presented. In addition to POR, three other 2-keto acid ferredoxin oxidoreductases are involved in peptide fermentation by hyperthermophilic archaea. It is proposed that the various aldehydes produced by these oxidoreductases in vivo are used by two aldehyde-utilizing enzymes, alcohol dehydrogenase and aldehyde ferredoxin oxidoreductase, the physiological roles of which were previously unknown.

show abstract

“…Hyperthermophiles are a recently discovered group of microorganisms that have the unusual property of growing optimally at temperatures near and even above 100ЊC (7,40). They have been isolated from geothermally heated environments, and most are of marine origin.…”

mentioning

confidence: 99%

Characterization of UDP amino sugars as major phosphocompounds in the hyperthermophilic archaeon Pyrococcus furiosus

1997

View full text Add to dashboard Cite

The archaeon Pyrococcus furiosus is a strictly anaerobic heterotroph that grows optimally at 100؇C by the fermentation of carbohydrates. It is known to contain high concentrations of novel intracellular solutes such as ␤-mannosylglycerate and di-myo-inositol 1,1-phosphate (DIP) (L. O. Martins and H. Santos, Appl. Environ. Microbiol. 61:3299-3303, 1995). Here, 31 P nuclear magnetic resonance (NMR) spectroscopy was used to show that this organism also accumulates another type of phospho compound, as revealed by a major multiplet signal in the pyrophosphate region. The compounds were purified from cell extracts of P. furiosus by anionexchange and gel filtration chromatographic procedures and were structurally analyzed by 1 H, 13 C, and 31 P NMR spectroscopy. They were identified as two uridylated amino sugars, UDP N-acetylglucosamine and UDP N-acetylgalactosamine. Unambiguous characterizations and complete assignments of 1 H and 13 C resonances from such sugars have not been previously reported. In vitro 31 P NMR spectroscopic analyses showed that, in contrast to DIP, which is maintained at a constant intracellular concentration (ϳ32 mM) throughout the growth phase of P. furiosus, the UDP amino sugars accumulated (to ϳ14 mM) only during the late log phase. The possible biochemical roles of these compounds in P. furiosus are discussed.Hyperthermophiles are a recently discovered group of microorganisms that have the unusual property of growing optimally at temperatures near and even above 100ЊC (7, 40). They have been isolated from geothermally heated environments, and most are of marine origin. Virtually all of them are classified under the domain Archaea rather than Bacteria (46). The domain Archaea includes some methanogenic and sulfate-reducing hyperthermophiles, but most of them are obligately anaerobic heterotrophs that reduce elemental sulfur (S 0 ) to H 2 S (2). The best studied of this group are members of the genus Pyrococcus (11). The type strain, Pyrococcus furiosus, is a marine organism that grows optimally at 100ЊC by the fermentation of peptides and carbohydrates. A variety of enzymes involved in the primary metabolic pathways of P. furiosus have been purified and characterized (1, 3).A key and, as yet, unresolved issue is how hyperthermophiles such as P. furiosus stabilize a wide range of biomolecules at extreme temperatures. This in turn has led to studies to determine if these organisms contain intracellular solutes that might have some general "thermoprotective" properties. This notion was first advanced by Scholz et al. (35), who found that Pyrococcus woesei maintains an intracellular potassium ion concentration of near 0.6 M and contains an equivalent concentration of the novel sugar di-myo-inositol-1,1Ј-phosphate (DIP) (Fig. 1). Moreover, under in vitro conditions, DIP was found to increase the thermal stability of an enzyme, glyceraldehyde-3-phosphate dehydrogenase, that has been purified from P. woesei (15,35). DIP is also present in the hyperthermophilic bacterium Thermotoga maritima (31) an...

show abstract

Isolation, taxonomy and phylogeny of hyperthermophilic microorganisms

Cited by 78 publications

References 53 publications

Compatible solutes of organisms that live in hot saline environments

Compatible solutes of organisms that live in hot saline environments

Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus , functions as a CoA-dependent pyruvate decarboxylase

Characterization of UDP amino sugars as major phosphocompounds in the hyperthermophilic archaeon Pyrococcus furiosus

Contact Info

Product

Resources

About