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Maria Garber - One of the best experts on this subject based on the ideXlab platform.
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The solution structure of ribosomal protein L36 from Thermus thermophilus reveals a zinc-ribbon-like fold.
Journal of Molecular Biology, 2000Co-Authors: Torleif Härd, Peter Allard, Lars Kloo, Maria GarberAbstract:We have determined the solution NMR structure of the ribosomal protein L36 from Thermus thermophilus. L36 is the smallest protein in the large subunit of the prokaryotic ribosome. The sequence cont ...
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Solution structure of the ribosomal protein S19 from Thermus thermophilus.
Journal of Molecular Biology, 1999Co-Authors: Magnus Helgstrand, Maria Garber, Natalia Davydova, Peter Allard, Torleif HärdAbstract:Ribosomal protein S19 is a 10.6 kDa protein in the small subunit of the prokaryotic ribosome. We have determined a high-resolution solution structure of S19 from Thermus thermophilus. Structures were calculated using 1160 distance and dihedral angle restraints derived from 1H, 15N and 13C NMR spectra. The structures show that S19 is a mixed α/β protein with long disordered tails. The folding topology is not homologous to that of any other known protein structure. Potential rRNA and protein binding sites have been identified on the S19 surface.
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Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli
FEBS Letters, 1997Co-Authors: Natalia Davydova, Olga I. Gryaznova, Bengt-harald Jonsson, Anders Liljas, Helena Berglund, Torleif Härd, Maria GarberAbstract:The gene for the ribosomal protein S19 from Thermus thermophilus was cloned, sequenced and overexpressed in Escherichia coli. A simple procedure for isolating the recombinant protein was developed. Preliminary NMR studies revealed a high content of α-helical secondary structure in the protein.
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Overexpression of the gene of ribosomal protein L30 from Thermus thermophilus and crystallization of the recombinant protein.
Biochemistry, 1997Co-Authors: Khairullina Ar, Stanislav Nikonov, Dmitry Shcherbakov, Svetlana Tishchenko, Maria GarberAbstract:: Ribosomal protein L30 from Thermus thermophilus was overexpressed in E. coli cells. The recombinant protein was isolated and crystallized. The crystals belong to the spatial group P3(1) 12, and their crystallographic parameters are not different from those of crystals obtained earlier from the ribosomal protein isolated from T. thermophilus.
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Ribosomal protein L22 from Thermus thermophilus: sequencing overexpression and crystallisation
FEBS Letters, 1995Co-Authors: Natalia Davydova, Olga I. Gryaznova, Oksana V. Mashchenko, Valentina S. Vysotskaya, Bengt-harald Jonsson, Salam Al-karadaghi, Anders Liljas, Maria GarberAbstract:Abstract The gene for the ribosomal protein L22 from Thermus thermophilus has been sequenced and overexpressed in Escherichia coli. A multiple sequence alignment was carried out for all proteins of the L22 family reported so far. The recombinant protein was purified and crystallized. The crystals belong to the space group P212121 with cell parameters of a = 32.6 A b = 66.0 A , c = 67.8 A .
Daniela Stock - One of the best experts on this subject based on the ideXlab platform.
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the structure of the peripheral stalk of Thermus thermophilus h atpase synthase
Nature Structural & Molecular Biology, 2010Co-Authors: Alastair G Stewart, Mhairi Donohoe, Ricardo A Bernal, Daniela StockAbstract:The crystal structure of the peripheral stalk of the A-type ATPase/synthase (A-ATPase) from Thermus thermophilus reveals a heterodimeric right-handed coiled coil, a protein fold never observed before. Fitting of the stalk structure into the EM density of intact A-ATPase provides the most complete composite model so far.
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The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase
Nature Structural & Molecular Biology, 2010Co-Authors: Alastair G Stewart, Mhairi Donohoe, Ricardo A Bernal, Daniela StockAbstract:The crystal structure of the peripheral stalk of the A-type ATPase/synthase (A-ATPase) from Thermus thermophilus reveals a heterodimeric right-handed coiled coil, a protein fold never observed before. Fitting of the stalk structure into the EM density of intact A-ATPase provides the most complete composite model so far.
Torleif Härd - One of the best experts on this subject based on the ideXlab platform.
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The solution structure of ribosomal protein L36 from Thermus thermophilus reveals a zinc-ribbon-like fold.
Journal of Molecular Biology, 2000Co-Authors: Torleif Härd, Peter Allard, Lars Kloo, Maria GarberAbstract:We have determined the solution NMR structure of the ribosomal protein L36 from Thermus thermophilus. L36 is the smallest protein in the large subunit of the prokaryotic ribosome. The sequence cont ...
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Solution structure of the ribosomal protein S19 from Thermus thermophilus.
Journal of Molecular Biology, 1999Co-Authors: Magnus Helgstrand, Maria Garber, Natalia Davydova, Peter Allard, Torleif HärdAbstract:Ribosomal protein S19 is a 10.6 kDa protein in the small subunit of the prokaryotic ribosome. We have determined a high-resolution solution structure of S19 from Thermus thermophilus. Structures were calculated using 1160 distance and dihedral angle restraints derived from 1H, 15N and 13C NMR spectra. The structures show that S19 is a mixed α/β protein with long disordered tails. The folding topology is not homologous to that of any other known protein structure. Potential rRNA and protein binding sites have been identified on the S19 surface.
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Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli
FEBS Letters, 1997Co-Authors: Natalia Davydova, Olga I. Gryaznova, Bengt-harald Jonsson, Anders Liljas, Helena Berglund, Torleif Härd, Maria GarberAbstract:The gene for the ribosomal protein S19 from Thermus thermophilus was cloned, sequenced and overexpressed in Escherichia coli. A simple procedure for isolating the recombinant protein was developed. Preliminary NMR studies revealed a high content of α-helical secondary structure in the protein.
Takayuki Hoshino - One of the best experts on this subject based on the ideXlab platform.
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Efficient Selection for Thermostable Protease in Thermus thermophilus
Bioscience Biotechnology and Biochemistry, 2020Co-Authors: Hiroshi Takagi, Takayuki Hoshino, Akitoshi Suzumura, Yoshiyuki Hasuura, Shigeru NakamoriAbstract:An efficient procedure was established to select for thermostable proteases in an extreme thermophile, Thermus thermophilus. A non-protease-secreting mutant derived from T. thermophilus TH125 was used as host and the expression plasmid for aqualysin I from T. aquaticus YT-1 was constructed as a source of thermostable protease. T. thermophilus cells harboring the recombinant plasmid produced active aqualysin I into the medium and were able to grow on a minimal medium containing milk casein as the sole source of carbon and nitrogen.
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Development of expression vectors for Thermus thermophilus
Journal of Fermentation and Bioengineering, 1998Co-Authors: Hideaki Maseda, Takayuki HoshinoAbstract: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 than the wild type.
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THERMOZEAXANTHINS, NEW CAROTENOID-GLYCOSIDE-ESTERS FROM THERMOPHILIC EUBACTERIUM Thermus thermophilus
Tetrahedron Letters, 1995Co-Authors: Akihiro Yokoyama, Takayuki Hoshino, Gerhard Sandmann, Kyoko Adachi, Miho Sakai, Yoshikazu ShizuriAbstract:Abstract New zeaxanthin-(di)glucoside-branched fatty acid esters, thermozeaxanthin-13, −15, and −17 ( 1–3 ), thermobiszeaxanthin-13-13, −13–15, and −15-15 ( 4–6 ) were isolated from the thermophilic eubacterium Thermus thermophilus . Their structures were determined by spectral means. The membrane of this thermophilic bacterium is thought to be stabilized by these carotenoids.
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Molecular cloning and sequence analysis of the proBA operon from an extremely thermophilic eubacterium Thermus thermophilus
Fems Microbiology Letters, 1994Co-Authors: Takehide Kosuge, Kazuyuki Tabata, Takayuki HoshinoAbstract:A 3.6 kb DNA fragment carrying the Thermus thermophilus proBA region, which encodes the first two steps in the proline biosynthetic pathway, was cloned from the Thermus thermophilus gene library, and its complete nucleotide sequence was determined. The deduced amino acid sequence of γ-glutamyl kinase (40,657 Da), the product of proB gene, and γ-glutamyl phosphate reductase (48, 747 Da), the product of proA gene, showed 44.1% and 44.4% identity to those of Escherichia coli, respectively. The termination codon of the proB gene and the initiation codon of the proA gene overlapped by 2 bp. A possible transcriptional termination structure was found downstream of the proA gene but not downstream of the proB gene. These results indicate that the proBA genes of T. thermophilus from a single operon as in E. coli.
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Overproduction of carotenoids in Thermus thermophilus
Journal of Fermentation and Bioengineering, 1994Co-Authors: Takayuki Hoshino, Ryouji Fujii, Tadaatsu NakaharaAbstract:Phytoene synthase encoded by the crtB gene is one of the rate-limiting enzymes for carotenoid production in Thermus thermophilus. We introduced a multicopy recombinant plasmid, pCOP1, in which the Thermus crtB gene was cloned, into carotenoid overproducing mutants of T. thermophilus. The overproducing mutants carrying a pCOP1 produced about twenty times as much carotenoids as the parental strain did.
Alexander S Spirin - One of the best experts on this subject based on the ideXlab platform.
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Ribosomal protein S1 from Thermus thermophilus: its detection, identification and overproduction.
FEBS letters, 2002Co-Authors: Vyacheslav M Shiryaev, Olga M Selivanova, Thomas Hartsch, Igor V Nazimov, Alexander S SpirinAbstract:Ribosomal protein S1 has been identified in Thermus thermophilus ribosomes. The gene of ribosomal protein S1 from Thermus thermophilus has been cloned and overexpressed in Escherichia coli. A procedure for purification of the protein has been developed.
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Formation and crystallization of Thermus thermophilus 70S ribosome/tRNA complexes.
FEBS Letters, 1991Co-Authors: Gulnara Yusupova, Alexander S Spirin, Marta Yusupov, Jean-pierre Ebel, Dino Moras, Chantal Ehresmann, Bernard EhresmannAbstract:70S ribosomes from Thermus thermophilus are able to form ternary complexes with N-AcPhe-tRNAPhe from either Thermus thermophilus or Escherichia coli, in the presence of a short oligo(U) of six or nine uridines. A complex of N-AcPhe-tRNAPhe/(U)9/70S ribosome from Th. thermophilus was crystallized under the same conditions used for the growth of crystals from isolated ribosomes (S.D. Trakhanov, et al., (1987) FEBS Lett. 220, 319–322).
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Thermus thermophilus ribosomes for crystallographic studies
Biochimie, 1991Co-Authors: M M Yusupov, V D Vasiliev, Maria Garber, Alexander S SpirinAbstract:Abstract Three-dimensional crystal of the 70S ribosomes, the 70S ribosome-mRNA-tRNA complex, the 30S ribosomal subunits, several ribosomal proteins, the elongation factor G and thronyl- and seryl-tRNA synthesis from a Gram-negative extreme thermophilic bacterium, Thermus thermophilus, have been obtained at our institute. X-ray and neutronographic data from the 70S ribosome crystals have been collected up to 18 A and 60 A, respectively. Two-dimensional crystalline sheets of the 70S ribosomes have been studied by electron microscopy. Structural studies of crystals of 2 ribosomal proteins, L1 and S6, elongation factor G and threonyl- and seryl-tRNA synthetases are also in progress. At present, Thermus thermophilus seems to be the most suitable microorganism to isolate ribosomes and their constituents for crystallographic studies.