Overproduction, Purification and Structural Studies on the Zn Containing S14 Ribosomal Protein from Thermus thermophilus

2000 ◽  
pp. 273-288
Author(s):  
P. Tsiboli ◽  
D. Triantafillidou ◽  
F. Leontiadou ◽  
M. Simitsopoulou ◽  
K. Anagnostopoulos ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Thermus Thermophilus ◽  
Structural Studies

scholarly journals The folate-binding module ofThermus thermophiluscobalamin-dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'

2018 ◽  
Vol 74 (1) ◽  
pp. 41-51
Author(s):  
Kazuhiro Yamada ◽  
Markos Koutmos
Keyword(s):  
Tertiary Amine ◽  
Thermus Thermophilus ◽  
Methionine Synthase ◽  
Structural Studies ◽  
Binding Domains ◽  
Methyl Transfer ◽  
Structural Differences ◽  
Tim Barrel ◽  
Eukaryotic Organisms

Methyl transfer between methyltetrahydrofolate and corrinoid molecules is a key reaction in biology that is catalyzed by a number of enzymes in many prokaryotic and eukaryotic organisms. One classic example of such an enzyme is cobalamin-dependent methionine synthase (MS). MS is a large modular protein that utilizes an SN2-type mechanism to catalyze the chemically challenging methyl transfer from the tertiary amine (N5) of methyltetrahydrofolate to homocysteine in order to form methionine. Despite over half a century of study, many questions remain about how folate-dependent methyltransferases, and MS in particular, function. Here, the structure of the folate-binding (Fol) domain of MS fromThermus thermophilusis reported in the presence and absence of methyltetrahydrofolate. It is found that the methyltetrahydrofolate-binding environment is similar to those of previously described methyltransferases, highlighting the conserved role of this domain in binding, and perhaps activating, the methyltetrahydrofolate substrate. These structural studies further reveal a new distinct and uncharacterized topology in the C-terminal region of MS Fol domains. Furthermore, it is found that in contrast to the canonical TIM-barrel β8α8fold found in all other folate-binding domains, MS Fol domains exhibit a unique β8α7fold. It is posited that these structural differences are important for MS function.

Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli

FEBS Letters ◽  
1997 ◽  
Vol 415 (2) ◽  
pp. 155-159 ◽  
Author(s):  
Natalia L Davydova ◽  
Alexey V Rak ◽  
Olga I Gryaznova ◽  
Anders Liljas ◽  
Bengt-Harald Jonsson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Thermus Thermophilus ◽  
Nmr Studies ◽  
Ribosomal Protein S19

scholarly journals The ribosomal protein S8 from Thermus thermophilus VK1. Sequencing of the gene, overexpression of the protein in Escherichia coli and interaction with rRNA

1994 ◽  
Vol 223 (2) ◽  
pp. 437-445 ◽  
Author(s):  
Valentina VYSOTSKAYA ◽  
Svetlana TISCHENKO ◽  
Maria GARBER ◽  
Daniel KERN ◽  
Marylene MOUGEL ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Thermus Thermophilus ◽  
Gene Overexpression

Ribosomal Protein S15 from Thermus Thermophilus. Cloning, Sequencing, Overexpression of the Gene and RNA-Binding Properties of the Protein

1997 ◽  
Vol 246 (2) ◽  
pp. 291-300 ◽  
Author(s):  
Alexander Serganov ◽  
Alexey Rak ◽  
Maria Garber ◽  
Joseph Reinbolt ◽  
Bernard Ehresmann ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Rna Binding ◽  
Thermus Thermophilus ◽  
Binding Properties ◽  
Ribosomal Protein S15

scholarly journals Crystal structure of the ribosomal protein S6 from Thermus thermophilus.

1994 ◽  
Vol 13 (6) ◽  
pp. 1249-1254 ◽  
Author(s):  
M. Lindahl ◽  
L.A. Svensson ◽  
A. Liljas ◽  
S.E. Sedelnikova ◽  
I.A. Eliseikina ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ribosomal Protein ◽  
Thermus Thermophilus ◽  
Ribosomal Protein S6

Isolation and Characterization of a New Ribosomal Protein from the Thermophilic Eubacteria,Thermus thermophilus, T. aquaticusandT. flavus

1993 ◽  
Vol 374 (1-6) ◽  
pp. 377-384 ◽  
Author(s):  
Theodora CHOLI ◽  
Francois FRANCESCHI ◽  
Ada YONATH ◽  
Brigitte WITTMANN-LIEBOLD
Keyword(s):  
Ribosomal Protein ◽  
Thermus Thermophilus ◽  
Isolation And Characterization

Identification of Ribosomal Protein L1-Binding Sites in Thermus thermophilus and Thermotoga maritima mRNAs

2018 ◽  
Vol 52 (1) ◽  
pp. 84-90
Author(s):  
A. O. Mikhaylina ◽  
O. S. Kostareva ◽  
E. Y. Nikonova ◽  
M. B. Garber ◽  
S. V. Tishchenko
Keyword(s):  
Ribosomal Protein ◽  
Binding Sites ◽  
Thermotoga Maritima ◽  
Thermus Thermophilus ◽  
Ribosomal Protein L1

Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable Fragment

2020 ◽  
Vol 85 (3) ◽  
pp. 344-354 ◽  
Author(s):  
S. Yu. Grishin ◽  
U. F. Dzhus ◽  
O. M. Selivanova ◽  
V. A. Balobanov ◽  
A. K. Surin ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Ribosomal Protein ◽  
Thermus Thermophilus

Conformation of Thermus thermophilus ribosomal protein S1 in solution at different ionic strengths

BIOPHYSICS ◽  
2007 ◽  
Vol 52 (2) ◽  
pp. 162-167 ◽  
Author(s):  
A. A. Timchenko ◽  
V. M. Shiryaev ◽  
Yu. Yu. Fedorova ◽  
H. Kihara ◽  
K. Kimura ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Thermus Thermophilus ◽  
Ribosomal Protein S1

Domain II of Thermus thermophilus Ribosomal Protein L1 Hinders Recognition of Its mRNA

2008 ◽  
Vol 383 (2) ◽  
pp. 301-305 ◽  
Author(s):  
Svetlana Tishchenko ◽  
Vladislav Kljashtorny ◽  
Olga Kostareva ◽  
Natalia Nevskaya ◽  
Alexei Nikulin ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Thermus Thermophilus ◽  
Ribosomal Protein L1
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