A deeply branching thermophilic bacterium with an ancient acetyl-CoA pathway dominates a subsurface ecosystem [PDF]
A nearly complete genome sequence of Candidatus ‘Acetothermum autotrophicum’, a presently uncultivated bacterium in candidate division OP1, was revealed by metagenomic analysis of a subsurface thermophilic microbial mat community.
A Stamatakis+69 more
core +17 more sources
Thermus thermophilus as a Source of Thermostable Lipolytic Enzymes [PDF]
Lipolytic enzymes, esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3), catalyze the hydrolysis of ester bonds between alcohols and carboxylic acids, and its formation in organic media.
Cerdán, María Esperanza+2 more
core +10 more sources
Transferable denitrification capability of thermus thermophilus [PDF]
Laboratory-adapted strains of Thermus spp. have been shown to require oxygen for growth, including the model strains T. thermophilus HB27 and HB8. In contrast, many isolates of this species that have not been intensively grown under laboratory conditions
Berenguer, José+4 more
core +6 more sources
NMR Solution Structure of the N-Terminal GSPII Domain from the Thermus Thermophilus Traffic ATPase PilF and Reconstruction of its c-di-GMP Binding Capability. [PDF]
GSPII‐A is the first of three consecutive GSPII domains of PilF from Thermus thermophilus and the only one that does not bind c‐di‐GMP. In this study we solve the structure of GSPII‐A and show the key factors hindering c‐di‐GMP binding. Through mutagenesis, we elucidate the minimal motif conservation needed for c‐di‐GMP recognition. Abstract The cyclic
Neißner K+7 more
europepmc +2 more sources
Thermus thermophilus genome analysis: benefits and implications [PDF]
The genome sequence analysis of Thermus thermophilus HB27, a microorganism with high biotechnological potential, has recently been published. In that report, the chromosomal and the megaplasmid sequence were compared to those of other organisms and discussed on the basis of their physiological and metabolic features.
Efthimia Lioliou+2 more
openaire +5 more sources
Tiamulin-Resistant Mutants of the Thermophilic Bacterium Thermus thermophilus. [PDF]
Tiamulin is a semisynthetic pleuromutilin antibiotic that binds to the 50S ribosomal subunit A site and whose (((2-diethylamino)ethyl)thio)-acetic acid tail extends into the P site to interfere with peptide bond formation. We have isolated spontaneous tiamulin-resistant mutants of the thermophilic bacterium Thermus thermophilus, containing either ...
Killeavy EE, Jogl G, Gregory ST.
europepmc +6 more sources
Allosteric Inhibition of Thermus Thermophilus Phosphofructokinase [PDF]
Thermus thermophilus phosphofructokinase (TtPFK) comes from an extreme thermophile and exhibits entropically-driven inhibition by phosphoenolpyruvate (PEP). Interestingly, a PFK from the moderate thermophile Bacillus stearothermophilus also exhibits entropically-driven inhibition, while enthalphically-driven inhibition is observed for PFK from ...
Maria Shubina-McGresham+1 more
openaire +2 more sources
Unconventional lateral gene transfer in extreme thermophilic bacteria [PDF]
Conjugation and natural competence are two major mechanisms that explain the acquisition of foreign genes throughout bacterial evolution. In recent decades, several studies in model organisms have revealed in great detail the steps involved in such ...
Carlos Bricio+5 more
core +4 more sources
Thiostrepton-resistant mutants of Thermus thermophilus [PDF]
Ribosomal protein L11 and its associated binding site on 23S rRNA together comprise one of the principle components that mediate interactions of translation factors with the ribosome. This site is also the target of the antibiotic thiostrepton, which has been proposed to act by preventing important structural transitions that occur in this region of ...
Dale M. Cameron+4 more
openaire +3 more sources
A DING phosphatase in Thermus thermophilus
Phosphate transport in bacteria occurs via a phosphate specific transporter system (PSTS) that belongs to the ABC family of transporters, a multisubunit system, containing an alkaline phosphatase. DING proteins were characterized due to the N-terminal amino acid sequence DINGG GATL, which is highly conserved in animal and plant isolates, but more ...
Pantazaki, A. A.+2 more
openaire +4 more sources