Results 201 to 210 of about 24,101 (229)

The growth behaviour of Thermus aquaticus in continuous cultivation

European Journal of Applied Microbiology and Biotechnology, 1982
The growth of the yellow pigmented non-sporulating caldoactive bacterium Thermus aquaticus was investigated in different culture vessels and using differnt culture techniques. Each combination of these two variables led to very specific characteristic behaviour of the culture. A synthetic medium for a white cell type of T.
S. Cometta, Armin Fiechter, Bernhard Sonnleitner   +2 more
openaire   +2 more sources

Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus.

Biochemical and Biophysical Research Communications, 2014
The thermophilic bacterium Thermus aquaticus is a well-known source of Taq polymerase. Here, we studied the structure and dynamics of the T. aquaticus cold-shock protein (Ta-Csp) to better understand its thermostability using NMR spectroscopy. We found that Ta-Csp has a five-stranded β-barrel structure with five salt bridges which are important for ...
Bonghwan Jin, K. Jeong, Yangmee Kim
semanticscholar   +4 more sources

Thermal stability of ribosomes and RNA from Thermus aquaticus

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1970
Abstract This paper presents data on the physical and chemical properties of the ribosomes and RNA of Thermus aquaticus, an organism able to grow at temperatures up to 79°. Ultracentrifugal analysis of purified ribosomes in 0.01 M Mg2+ demonstrated components sedimenting at 50 S, 70 S and 100 S.
Thomas D. Brock, J.G. Zeikus, Milton W. Taylor   +2 more
openaire   +2 more sources

Cloning and Sequencing of the Thermus aquaticus Glycerol Facilitator Gene

DNA Sequence, 2002
The gene glpK, encoding glycerol kinase of Thermus aquaticus has been identified [Biosci. Biotechnol. Biochem., 62 (1998) 2375-2381]. In the present work, the nucleotide sequence of glpFK operon and the gene glpF encoding glycerol facilitator were determined. T.
Tadashi Yoshimoto, Hua-Shan Huang, Kiyoshi Ito   +2 more
openaire   +3 more sources

large fragment of DNA Polymerase I from Thermus aquaticus in a closed ternary complex with the natural base pair 5fC:dGTP

, 2018
The emergence of unnatural DNA bases provides opportunities to demystify the mechanisms by which DNA polymerases faithfully decode chemical information on the template. It was previously shown that two unnatural cytosine bases (termed "M-fC" and "I-fC"),
Chengqi Yi, Hongmei Zeng, M. Mondal, R. Song, Jing Zhang, B. Xia, Miao Liu, Chenxu Zhu, B. He, Yi Qin Gao   +9 more
semanticscholar   +1 more source

Recombinant Thermus aquaticus RNA Polymerase for Structural Studies

Journal of Molecular Biology, 2006
Advances in the structural biology of bacterial transcription have come from studies of RNA polymerases (RNAPs) from the thermophilic eubacteria Thermus aquaticus (Taq) and Thermus thermophilus (Tth). These structural studies have been limited by the fact that only endogenous Taq or Tth RNAP, laboriously purified from large quantities of Taq or Tth ...
Konstantin Kuznedelov, Seth A. Darst, Valérie Lamour, Georgia A. Patikoglou, Mark Chlenov, Konstantin Severinov   +5 more
openaire   +3 more sources

Rapid Arsenite Oxidation by Thermus aquaticus and Thermus thermophilus:  Field and Laboratory Investigations

Environmental Science & Technology, 2001
Thermus aquaticus and Thermus thermophilus, common inhabitants of terrestrial hot springs and thermally polluted domestic and industrial waters, have been found to rapidly oxidize arsenite to arsenate. Field investigations at a hot spring in Yellowstone National Park revealed conserved total arsenic transport and rapid arsenite oxidation occurring ...
Jillian F. Banfield, Gregory K. Druschel, Robert J. Hamers, Thomas M. Gihring, R B McCleskey   +4 more
openaire   +2 more sources

Purification and Properties of Malate Dehydrogenase from Thermus Aquaticus

1976
The extreme thermophile Thermus aquaticus 1 grows optimally at 70° to a high cell density with a mean generation time of about one hour. The type strain YT1, and several strains of similar genera and species have been used for the purification of enzymes for comparison with those of mesophiles2. We have purified and investigated malate dehydrogenase (E.
J. H. F. Biffen, R. A. D. Williams
openaire   +3 more sources

Preparation and Characterization of Recombinant Thermus aquaticus RNA Polymerase

2003
Publisher Summary This chapter reviews the overproduced thermus aquaticus (Taq) RNAP subunits that are assembled in functional RNAP in vitro and in vivo when coexpressed in E. coli. Binding of the core enzyme, consists of the five core subunits—β´, β, a dimer of identical α subunits, and the ω subunit.
Konstantin D. Kuznedelov, Leonid Minakhin, Konstantin Severinov   +2 more
openaire   +3 more sources

Preliminary crystallographic study ofThermus aquaticusglycerol kinase

Acta Crystallographica Section D Biological Crystallography, 2001
Glycerol kinase (GlpK) is an important enzyme which catalyzes the rate-limiting step in a central biochemical pathway involving glycerol metabolism. GlpK from the thermophile Thermus aquaticus has been overexpressed in glpK-deficient Escherichia coli and crystallized by the hanging-drop method.
Hua-Shan Huang, Takahiko Inoue, Kiyoshi Ito, Tadashi Yoshimoto   +3 more
openaire   +3 more sources