Library Generation and Auxotrophic Selection Assays in Escherichia coli and Thermus thermophilus

2017 ◽  
pp. 333-345
Author(s):  
Jörg Claren ◽  
Thomas Schwab ◽  
Reinhard Sterner
Keyword(s):  
Escherichia Coli ◽  
Thermus Thermophilus

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

Cloning and expression of the leucine gene from Thermus thermophilus in Escherichia coli

Gene ◽  
1980 ◽  
Vol 10 (2) ◽  
pp. 137-145 ◽  
Author(s):  
Nagahari Kenji ◽  
Koshikawa Takako ◽  
Sakaguchi Kenji
Keyword(s):  
Escherichia Coli ◽  
Thermus Thermophilus ◽  
Cloning And Expression

scholarly journals Characterization of the protein gp1 from bacteriophage φIN93

2011 ◽  
Vol 48 (1) ◽  
pp. 47-56 ◽  
Author(s):  
Isao Matsushita ◽  
Hideshi Yanase
Keyword(s):  
Escherichia Coli ◽  
Recombinant Plasmid ◽  
Shuttle Vector ◽  
Thermus Thermophilus ◽  
The Other ◽  
Replication Protein

Characterization of the protein gp1 from bacteriophage φIN93The protein gp1, encoded by theORF1gene in the genome of theThermusphage φIN93, is similar to the replication protein encoded byrepAin theThermus sp.plasmid. To confirm that gp1 functions as a replication protein, we constructed the recombinant plasmid pIA1, by insertingORF1and the kanamycin acetyltransferase (kat) gene into pBluescriptII SK(+), which enabled replication of pIA1 inThermus thermophilusHB27. By contrast, plasmid pIA1-del, which contained only a part ofORF1(the other part deleted usingKpnI), was not replicated. These results show that gp1 functions as a replication protein and that pIA1 can be used as a shuttle vector betweenThermus thermophilusHB27 andEscherichia coli.

scholarly journals Comparative study of subunits of phenylalanyl-tRNA synthetase from Escherichia coli and Thermus thermophilus

FEBS Letters ◽  
1991 ◽  
Vol 290 (1-2) ◽  
pp. 95-98 ◽  
Author(s):  
Ekaterina V. Bobkova ◽  
Anton V. Mashanov-Golikov ◽  
Aleksey Wolfson ◽  
Valentina N. Ankilova ◽  
Olga I. Lavrik
Keyword(s):  
Escherichia Coli ◽  
Comparative Study ◽  
Thermus Thermophilus ◽  
Trna Synthetase

scholarly journals An angular motion of a conserved four-helix bundle facilitates alternating access transport in the TtNapA and EcNhaA transporters

2020 ◽  
Vol 117 (50) ◽  
pp. 31850-31860
Author(s):  
Gal Masrati ◽  
Ramakanta Mondal ◽  
Abraham Rimon ◽  
Amit Kessel ◽  
Etana Padan ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Conformational Change ◽  
Thermus Thermophilus ◽  
Angular Motion ◽  
Cross Linking ◽  
Conformational Sampling ◽  
Ongoing Debate ◽  
Helix Bundle ◽  
Bias Potential ◽  
Alternating Access

There is ongoing debate regarding the mechanism through which cation/proton antiporters (CPAs), like Thermus thermophilus NapA (TtNapA) and Escherichia coli NapA (EcNhaA), alternate between their outward- and inward-facing conformations in the membrane. CPAs comprise two domains, and it is unclear whether the transition is driven by their rocking-bundle or elevator motion with respect to each other. Here we address this question using metadynamics simulations of TtNapA, where we bias conformational sampling along two axes characterizing the two proposed mechanisms: angular and translational motions, respectively. By applying the bias potential for the two axes simultaneously, as well as to the angular, but not the translational, axis alone, we manage to reproduce each of the two known states of TtNapA when starting from the opposite state, in support of the rocking-bundle mechanism as the driver of conformational change. Next, starting from the inward-facing conformation of EcNhaA, we sample what could be its long-sought-after outward-facing conformation and verify it using cross-linking experiments.

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