Thermus thermophilus

Yokoyama, A., G. Sandmann, T. Hoshino, K. Adachi, M. Sakai, and Y. Shizuri. 1995. Thermozeaxanthins, new carotenoid-glycoside-esters from thermophilic eubacterium Thermus thermophilus. Tetrahedron Lett. 36 4901 1904. 

Angelini, S., Moreno, R., Gouffi, K. et al. (2001) Export of Thermus thermophilus alkaline phosphatase via the twin-arginine translocation pathway in Escherichia coli. FEBS Letters, 506 (2), 103-107. 

Hagen, W.R., Dunham, W.R., Johnson, M.K., and Fee, J.A. 1985a. Quarter field resonance and integer-spin/half-spin interaction in the EPR of Thermus thermophilus ferredoxin. Possible new fingerprints for three iron clusters. Biochimica et Biophysica Acta 828 369-374. 

M.S. Lah, M.M. Dixon, K.A. Pattridge, W.C. Stallings, J.A. Fee, and M.L. Ludwig, Structure-function in Escherichia coli iron superoxide dismutase comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry. 34, 1646-1660 (1995). 

RNA amplification by PCR has been facilitated by the use of a single heat-stable enzyme. Thus, DNA polymerase from Thermus thermophilus, which has enhanced reverse transcriptase (rT) activity in presence of manganese, can be used with one buffer system. The high temperature used for rT (70°C) to produce a complementary DNA copy from RNA, and the subsequent amplification of DNA at 60°C, increases efficiency by destabilizing secondary structures in the RNA template. This procedure has been used for the amplification of hepatitis C viral RNA (Yl). 

Salminen, T., A. Teplyakov, J. Kankare, B.S. Cooperman, R. Lahti, and A. Goldman. 1996. An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic pyrophosphatases. Protein Sci 5 1014-1025. 

Kern, D., and Moras, D. Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus, Embo J 1995, 34, 4156-4167. 

Yoshida, M., and Moeikawa, K. Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8. Structure (Camb) 2002, 10, 1415-1423. 

Satoh T, Takahashi Y, Oshida N, Shimizu A, Shinoda H, et al. 1999. A chimeric inorganic pyrophosphatase derived from Escherichia coli and Thermus thermophilus has an increased thermostability. Biochemistry 38(5) 1531. 

Figure 10 The transamidosome of Thermus thermophilus catalyzing tRNA asparaginylation. (a) Formation of the transamidosome (I) The AspRS (in blue) binds tRNA " (in gray, Kq = 2 pmol l ) before association of the amidotransferase GatCAB (in orange, Kq = 0.6 pmol l ) to form the ternary complex, (ii) The free GatCAB binds tRNA " with a poor affinity (Kd > 10 pmol r ) before association of tRNA " thus pathway (i) is preferred forthe formation of the transamidosome. (b) The catalytic cycle of the transamidosome. In the absence of free tRNA ", the transamidosome aminoacylates tRNA " with a first-order rate constant of 0.017 s (1) and amidates the tRNA "-bound Asp into Asn with a rate constant of 0.11 s (2). In the presence of an excess of free tRNA ", the first Asn-tRNA " is formed with a rate constant of 0.094 s (3), whereas the following catalytic cycles occur with a rate constant of 0.043 s (4), indicating that dissociation of the newly formed Asn-tRNA " accompanied by the disruption of the complex is rate-limiting at the steady state.

M. -H. Mazauric, Le systeme de la glycylation de I ARNt de Thermus thermophilus. Etudes structurales et fonctionnelles et interrelation avec d autres systemes de glycylation. Ph.D. Thesis, Universite Louis Pasteur, Strasbourg, France, 1997. 

The ribosome recycling factor (RRF) is a 21 kDa protein which is involved in the termination step of protein biosynthesis and catalyses the breakdown of the post termination complex into ribosome, tRNA and mRNA. The solution structure of RRF from the hyperthermophilic bacterium Aquifex aeolicus (7 opt = 85°Q was determined by heteronuclear multidimensional NMR spectroscopy, whereas the backbone NMR assignment was recently carried out for RRF from Themotoga maritima and Thermus thermophilus ... 

Figure 3. MOssbauer spectra of the reduced Rieske protein Thermus Thermophilus. (A) Spectrum taken at 230 K. The brackets indicate the doublets of the trapped-valence Fe2+ and Fe3+ sites. (B) 4.2 K spectrum of the same sample. The solid line is a spectral simulation based on an S = 1/2 spin Hamiltonian. S = 1/2 is the system spin resulting from coupling S = Sa + Sb according to H = JSa-Sb for J > 0 Sa = 5/2 and Sb = 2.

Figure 3, UV-visible absorption and variable temperature MCD spectra for (a) oxidized and (b) partially reduced Thermus thermophilus ferredoxin.

Figure 4. MCD magnetization plots for (a) oxidized and (b) partially reduced Thermus thermophilus ferredoxin. Data collected at 1.55 K (x), 4.22 K (A), and 9-100 K ( ), with magnetic fields between 0 and 4.5 T.

Manganese is used by nature to catalyze a number of important biological reactions that include the dismutation of superoxide radicals, the decomposition of hydrogen peroxide, and the oxidation of water to dioxygen. The dinuclear manganese centers that occur in Lactobacillus plantar-aum catalase and Thermus thermophilus catalase have attracted considerable attention and many model compounds have now been synthesized that attempt to mimic aspects of these biological systems.The catalases have at least four accessible oxidation states (Mn Mn , Mn°Mn , Mn" Mn", and Mn Mn ) it is believed that the Mn"Mn"/Mn"Mn" redox couple is effective in catalyzing the disproportionation of water. 

Crystal structures of manganese catalases (in the (111)2 oxidation state) from Lactobacillus plantarum,its azide-inhibited complex, " and from Thermus thermophilus have been determined. There are differences between the structures that may reflect distinct biological functions for the two enzymes, the L. plantarum enzyme functions only as a catalase, while the T. thermo-philus enzyme may function as a catalase/peroxidase. The active sites are conserved in the two enzymes and are shown schematically in Figure 32. Each subunit contains an Mu2 active site,... 

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