Results 191 to 200 of about 6,413 (224)

A defined cultivation medium for Sulfolobus acidocaldarius

Journal of Biotechnology, 2019
The thermoacidophilic Crenarchaeon Sulfolobus acidocaldarius is an important model organism for Archaea and genetic systems are well established. To date, the organism is routinely cultivated on complex media based on protein hydrolysates and no common defined medium is established. In this work we address this lack of a standardized defined medium and
Julian Quehenberger, Andreas Albersmeier, Holger Glatzel, Matthias Hackl, Jörn Kalinowski, Oliver Spadiut   +5 more
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An infB-Homolog in Sulfolobus acidocaldarius

Systematic and Applied Microbiology, 1996
Summary We have identified an archaeal homologue of the bacterial translation initiation factor 2 (IF-2 or inf B) in a partial open reading frame situated upstream of the gene cluster coding for the large subunits of the DNA-dependent RNA polymerase (RNAP) in Sulfolobus acidocaldarius .
Patrick J. Keeling, Sandra L. Baldauf, W. Ford Doolittle, Wolfram Zillig, Hans-Peter Klenk   +4 more
openaire   +1 more source

Histone-like protein in the Archaebacterium Sulfolobus acidocaldarius

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1983
The Archaebacterium Thermoplasma acidophilum contains a basic chromosomal protein remarkably similar to the histones of eukaryotes. Therefore, it was of interest to examine a different Archaebacterium for similar proteins. We chose to examine Sulfolobus acidocaldarius because it is thermophilic, like T.
GREEN, GR, Searcy, DG, DELANGE, RJ
openaire   +3 more sources

Optimization of pyrite bioleaching using Sulfolobus acidocaldarius

Applied Microbiology and Biotechnology, 1993
Optimization of batch pyrite bioleaching with Sulfolobus acidocaldarius was performed using statistical modelling and experimental design. First a screening design was made followed by response surface modelling. The dominating factors identified were pH, pulp density and particle size. The highest batch leaching rate after optimization was 270 mg iron·
E. B�rje Lindstr�m, Svante Wold, Nouna Kettaneh-Wold, Siv S��f   +3 more
openaire   +1 more source

Thermopsin, A Thermostable Acid Protease from Sulfolobus Acidocaldarius

1991
Most of the well-studied aspartic proteases, including those derived from yeast, fungi, plants and animal sources, are stable in temperatures up to about 50° to 60°C. Aspartic proteases which can function at high temperature in the range of 80° to 100°C have not been reported so far.
X, Lin, M, Fusek, J, Tang
openaire   +2 more sources

Characterization of two β-decarboxylating dehydrogenases from Sulfolobus acidocaldarius

Extremophiles, 2016
Sulfolobus acidocaldarius, a hyperthermoacidophilic archaeon, possesses two β-decarboxylating dehydrogenase genes, saci_0600 and saci_2375, in its genome, which suggests that it uses these enzymes for three similar reactions in lysine biosynthesis through 2-aminoadipate, leucine biosynthesis, and the tricarboxylic acid cycle.
Takahashi, Kento, Nakanishi, Fumika, Tomita, Takeo, Akiyama, Nagisa, Lassak, Kerstin, Albers, Sonja Verena, Kuzuyama, Tomohisa, Nishiyama, Makoto   +7 more
openaire   +3 more sources

Membrane-bound ATPase of a thermoacidophilic archaebacterium, Sulfolobus acidocaldarius

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1985
The membranes of Sulfolobus, a thermoacidophilic archaebacterium showed two types of ATP hydrolyzing activity. One was that of a neutral ATPase at an optimum pH around 6.5. This enzyme was activated by 10 mM sulfate with a shift of optimum pH to 5.
T, Wakagi, T, Oshima
openaire   +2 more sources

A secY homologous gene in the crenarchaeon Sulfolobus acidocaldarius

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1995
The nucleotide sequence of an open reading frame, located upstream of the gene for adenylate kinase, was determined in the thermoacidophile crenarchaeon Sulfolobus acidocaldarius. Data bank searches identified the sequence as a secY homologous gene. The DNA derived protein sequence of total 463 amino acids contains 10 hydrophobic domains.
T, Kath, G, Schäfer
openaire   +2 more sources

Molecule and Gene of Sulfolobus acidocaldarius ATPase

1990
A novel ATPase (Sul-ATPase) was solubilized from membranes of an archaebacterium, Sulfolobus acidocaldarius, by washing with a buffer containing EDTA. Enzymatic characteristics of this ATPase are distinctly different from F1-ATPase and resemble eukaryotic endomembrane H+-ATPase.
Kimitoshi Denda, Jin Konishi, Kyoko Hajiro, Tairo Oshima, Takayasu Date, Masasuke Yoshida   +5 more
openaire   +1 more source

Purification and characterization of NADH oxidase from the archaea Sulfolobus acidocaldarius and Sulfolobus solfataricus

Biotechnology and Applied Biochemistry, 1996
The enzyme NADH oxidase (EC 1.6.99.3) has been isolated from the two thermoacidophilic archaea Sulfolobus acidocaldarius and Sulfolobus solfataricus and characterized. In both organisms the enzyme oxidizes specifically beta‐NADH in the presence of molecular oxygen and requires the presence of a flavin cofactor, showing a high specificity for FAD.
MASULLO, Mariorosario, RAIMO G, DELLO RUSSO A, BOCCHINI V, BANNISTER JV   +4 more
openaire   +4 more sources