Results 251 to 260 of about 40,909 (278)

Purification and characterization of Thermus thermophilus UvrD

Extremophiles, 2003
The DNA helicase UvrD (helicase II) protein plays an important role in nucleotide excision repair, mismatch repair, rolling circular plasmid replication, and in DNA replication. A homologue of the Escherichia coli uvrD gene was previously identified in Thermus thermophilus; however, to date, a UvrD helicase has not been purified and characterized from ...
Tommie V. McCarthy, Ruairi Collins
openaire   +2 more sources

The genome sequence of the extreme thermophile Thermus thermophilus

Nature Biotechnology, 2004
Thermus thermophilus HB27 is an extremely thermophilic, halotolerant bacterium, which was originally isolated from a natural thermal environment in Japan. This organism has considerable biotechnological potential; many thermostable proteins isolated from members of the genus Thermus are indispensable in research and in industrial applications.
Henne, Anke, Brüggemann, Holger, Raasch, Carsten, Wiezer, Arnim, Hartsch, Thomas, Liesegang, Heiko, Johann, Andre, Lienard, Tanja, Gohl, Olivia, Martinez-Arias, Rosa, Jacobi, Carsten, Starkuviene, Vytaute, Schlenczeck, Silke, Dencker, Silke, Huber, Robert, Klenk, Hans-Peter, Kramer, Wilfried, Merkl, Rainer, Gottschalk, Gerhard, Fritz, Hans-Joachim   +19 more
openaire   +5 more sources

[15] Chaperonin from thermophile Thermus thermophilus

1998
Publisher Summary The chapter describes the methods for manipulating the Thermus chaperonin. A unique chaperonin system using the chaperonin from one of the thermophilic eubacteria, Thermusthermophilus is developed. Although amino acid sequences of the chaperonin from T.
Taguchi, H., Yoshida, M.
openaire   +3 more sources

Isolation and Characterisation of the ylmE Homologue of Thermus thermophilus

DNA Sequence, 2001
Screening of a Thermus thermophilus genomic library led to the identification of a homologue of the ylmE gene. ylmE is highly conserved in widely divergent organisms from prokaryotes to mammals, suggesting an important, albeit currently unknown, cellular function.
Yann Gibert, J. Tony Pembroke, J. Gerard Wall, Stefania Spada   +3 more
openaire   +3 more sources

l-Alanine dehydrogenase from Thermus thermophilus

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
A heat-stable L-alanine dehydrogenase was isolated and purified from the extremely thermophilic microorganism, Thermus thermophilus, by affinity chromatography. The enzyme has a molecular weight of 290 000, as determined by the sedimentation equilibrium method, and is composed of six subunits of identical molecular weight as concluded from sodium ...
Susan Lakatos, Péter Závodszky, S.A. Venyaminov, Z. Váli, Ferenc Kilár   +4 more
openaire   +3 more sources

The Thermus thermophilus comEA/comEC operon is associated with DNA binding and regulation of the DNA translocator and type IV pili.

Environmental Microbiology, 2016
Natural transformation systems and type IV pili are linked in many naturally competent bacteria. In the Gram-negative bacterium Thermus thermophilus, a leading model organism for studies of DNA transporters in thermophilic bacteria, seven competence ...
Ralf Salzer, Timo Kern, Friederike Joos, B. Averhoff   +3 more
semanticscholar   +1 more source

Development of expression vectors for Thermus thermophilus

Journal of Fermentation and Bioengineering, 1998
We constructed expression vectors for Thermus thermophilus. The transformation efficiency of pTEV131 per viable cells was 0.15% at 60°C and 0.11% at 68°C, and with marker rescue transformation, it was 1.9% at 60°C and 0.5% at 68°C. When the crtB gene was inserted into the cloning sites of this vector, the transformant expressed 3-fold more crtB gene ...
Hideaki Maseda, Takayuki Hoshino
openaire   +2 more sources

A chaperonin from a thermophilic bacterium, Thermus thermophilus

Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 1993
Unlike Escherichia coli chaperonins, a chaperonin (cpn) from a therm ophilic bacterium , Thermus thermophilus , consisting of homologues to GroEL (cpn 60) and GroES (cpn 10) is co-purified as a large complex.
Masasuke Yoshida, Noriyuki Ishii, H. Saibil, Hideki Taguchi, Paul V. Viitanen, George H. Lorimer, R. Jaenicke, Eiro Muneyuki   +7 more
openaire   +4 more sources

Biotechnologically relevant enzymes from Thermus thermophilus

Applied Microbiology and Biotechnology, 2002
Enzymes produced by Thermus thermophilus are of considerable biotechnological interest. This review covers industrial applications of several protein products of this thermophilic bacterium that are functional under extreme conditions. The purification of proteins from T.
Agathi Pritsa, Anastasia A. Pantazaki, Dimitrios A. Kyriakidis   +2 more
openaire   +3 more sources

An Isochizomer of TaqI from Thermus thermophilus HB8

The Journal of Biochemistry, 1978
A site-specific endonuclease has been isolated from Thermus thermophilus HB8 and named TthHB8I. It recognizes the same sequences as TaqI from Thermus aquaticus YT-1 does. The amount of TthHB8I in the cells was comparable to that of TaqI. T. thermophilus HB8 has an advantage over T. aquaticus YT-1 for preparation of a TaqI-like enzyme since it is easier
Takahisa Shinomiya, Showbu Sato
openaire   +3 more sources