Results 111 to 120 of about 2,580 (147)

Effect of UV irradiation on Sulfolobus acidocaldarius and involvement of the general transcription factor TFB3 in the early UV response. [PDF]

Nucleic Acids Res, 2018
Schult F, Le TN, Albersmeier A, Rauch B, Blumenkamp P, van der Does C, Goesmann A, Kalinowski J, Albers SV, Siebers B.   +9 more
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Gene analysis of Sulfolobus acidocaldarius ATPase

, 1989
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Population ecology of Sulfolobus acidocaldarius

Archives of Microbiology, 1974
Optimal temperatures for elemental sulfur oxidation were determined for Sul/olobus acidocaldarius populations in a variety of hot, acid springs in Yellow- stone National Park, Wyoming. Cultures were obtained from some of the springs by enrichment and isolation at different incubation temperatures, and the optimal temperatures for these were also ...
B B Bohlool, Thomas D Brock, T D Brock
exaly   +5 more sources

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
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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
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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
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AmyA contributes to the glycogen synthesis in Sulfolobus acidocaldarius

International Journal of Biological Macromolecules
Glycogen, an α-1,4 linked glucose polymer with α-1,6 linked branches, accumulates in Sulfolobus acidocaldarius in granular form and contributes to stress resistance. While the glg operon responsible for glycogen metabolism has been studied, the gene responsible for branch formation remained elusive.
Areum, Lee, Nahyun, Park, Chihong, Song, Jaeho, Cha   +3 more
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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
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Structure of the S-layer of Sulfolobus acidocaldarius

Nature, 1982
The outermost component of many bacterial cell envelopes is a two-dimensional crystalline array of protein molecules, termed the S-layer1. Despite considerable effort to investigate its structure and composition, its precise function remains uncertain.
K. A. Taylor, J. F. Deatherage, L. A. Amos   +2 more
openaire   +1 more source