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Science 15 May 1987:
Vol. 236. no. 4803, pp. 822 - 824
DOI: 10.1126/science.236.4803.822
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Articles

Isolation of Extremely Thermophilic Sulfate Reducers: Evidence for a Novel Branch of Archaebacteria

KARL O. STETTER 1, GERTA LAUERER 1, MICHAEL THOMM 1, and ANNEMARIE NEUNER 1

1 Institut für Biochemie, Genetik und Mikrobiologie, Universität Regensburg, Universitätsstraße 31, D-8400 Regensburg, Federal Republic of Germany.

Extremely thermophilic archaebacteria are known to be metabolizers of elemental sulfur and the methanogens. A novel group of extremely thermophilic archaebacteria is described, which consists of sulfate-respiring organisms that contain pure factor 420 and that have been isolated from marine hydrothermal systems in Italy. They possess a third type of archaebacterial RNA polymerase structure previously unknown, indicating an exceptional phylogenetic position. Most likely, this group represents a third major branch within the archaebacteria. The existence of sulfate reducers at extremely high temperatures could explain hydrogen sulfide formation in hot sulfate-containing environments, such as submarine hydrothermal systems and deep oil wells.

Submitted on December 1, 1986
Accepted on February 20, 1987


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Unusual Starch Degradation Pathway via Cyclodextrins in the Hyperthermophilic Sulfate-Reducing Archaeon Archaeoglobus fulgidus Strain 7324.
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Effect of Low Sulfate Concentrations on Lactate Oxidation and Isotope Fractionation during Sulfate Reduction by Archaeoglobus fulgidus Strain Z.
K. S. Habicht, L. Salling, B. Thamdrup, and D. E. Canfield (2005)
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Structural and functional analysis of the gpsA gene product of Archaeoglobus fulgidus: A glycerol-3-phosphate dehydrogenase with an unusual NADP+ preference.
S.-I. Sakasegawa, C. H. Hagemeier, R. K. Thauer, L.-O. Essen, and S. Shima (2004)
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A Novel Archaeal Alanine Dehydrogenase Homologous to Ornithine Cyclodeaminase and {micro}-Crystallin.
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Structural Basis for the Binding of Compatible Solutes by ProX from the Hyperthermophilic Archaeon Archaeoglobus fulgidus.
A. Schiefner, G. Holtmann, K. Diederichs, W. Welte, and E. Bremer (2004)
J. Biol. Chem. 279, 48270-48281
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Flavin Mononucleotide-Binding Flavoprotein Family in the Domain Archaea.
Y.-H. R. Ding and J. G. Ferry (2004)
J. Bacteriol. 186, 90-97
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Linkage of High Rates of Sulfate Reduction in Yellowstone Hot Springs to Unique Sequence Types in the Dissimilatory Sulfate Respiration Pathway.
S. Fishbain, J. G. Dillon, H. L. Gough, and D. A. Stahl (2003)
Appl. Envir. Microbiol. 69, 3663-3667
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Novel Type of ADP-Forming Acetyl Coenzyme A Synthetase in Hyperthermophilic Archaea: Heterologous Expression and Characterization of Isoenzymes from the Sulfate Reducer Archaeoglobus fulgidus and the Methanogen Methanococcus jannaschii.
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J. Bacteriol. 184, 636-644
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H2O2-Forming NADH Oxidase with Diaphorase (Cytochrome) Activity from Archaeoglobus fulgidus.
D. W. Reed, J. Millstein, and P. L. Hartzell (2001)
J. Bacteriol. 183, 7007-7016
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Comparison of Isocitrate Dehydrogenase from Three Hyperthermophiles Reveals Differences in Thermostability, Cofactor Specificity, Oligomeric State, and Phylogenetic Affiliation.
I. H. Steen, D. Madern, M. Karlstrom, T. Lien, R. Ladenstein, and N.-K. Birkeland (2001)
J. Biol. Chem. 276, 43924-43931
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Biogenicity of gold- and silver-bearing siliceous sinters forming in hot (75{degrees}C) anaerobic spring-waters of Champagne Pool, Waiotapu, North Island, New Zealand.
B. Jones, B. JONES, R. W. RENAUT, and M. R. ROSEN (2001)
Journal of the Geological Society 158, 895-911
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Some aspects of diagenetic sulphate-hydrocarbon redox reactions.
H. G. Machel (1987)
Geological Society, London, Special Publications 36, 15-28
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Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution.
G. Fritz, A. Roth, A. Schiffer, T. Buchert, G. Bourenkov, H. D. Bartunik, H. Huber, K. O. Stetter, P. M. H. Kroneck, and U. Ermler (2002)
PNAS 99, 1836-1841
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Science. ISSN 0036-8075 (print), 1095-9203 (online)