Oligomerization of a MutS Mismatch Repair Protein from Thermus aquaticus [PDF]
Journal of Biological Chemistry, 1999 The MutS DNA mismatch protein recognizes heteroduplex DNAs containing mispaired or unpaired bases. We have examined the oligomerization of a MutS protein from Thermus aquaticus that binds to heteroduplex DNAs at elevated temperatures. Analytical gel filtration, cross-linking of MutS protein with disuccinimidyl suberate, light scattering, and matrix ...
Indranil Biswas +7 more
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The crystal structure of the Thermus aquaticus DnaB helicase monomer. [PDF]
Nucleic Acids Res, 2007 The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork of eubacteria. We have solved the crystal structure of the full-length Thermus aquaticus DnaB monomer, or possibly dimer, at 2.9 A resolution. DnaB is a highly flexible two domain protein.
Bailey S, Eliason WK, Steitz TA.
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Succinate thiokinase from Thermus aquaticus and Halobacterium salinarium [PDF]
FEBS Letters, 1983 Both citrate synthase and succinate thiokinase occur in either a ‘large’ or ‘small’ form. The ‘large’ forms of these two enzymes have been found only in Gram‐negative bacteria, whereas Gram‐positive bacteria and eukaryotes contain the ‘small’ forms of the two.
P.D.J. Weitzman, Helen A. Kinghorn
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Structure of the GDP-bound state of the SRP GTPase FlhF. [PDF]
Acta Crystallogr F Struct Biol CommunThis study presents the X‐ray structure of FlhF in its GDP‐bound state at a resolution of 2.28 Å, exhibiting the classical N‐ and G‐domain fold. Comparative analysis with GTP‐loaded FlhF elucidates the conformational changes associated with GTP hydrolysis.The GTPase FlhF, a signal recognition particle (SRP)‐type enzyme, is pivotal for spatial–numerical
Dornes A, Mais CN, Bange G.
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Structural Evolution of Bacterial Polyphosphate Degradation Enzyme for Phosphorus Cycling. [PDF]
Adv Sci (Weinh)This study demonstrates an interdomain linker‐based exopolyphosphatase (PPX) structural evolution in bacteria. The length of ɑ‐linker in PPX, which involves phosphate cycling, is varied among bacteria and has impacts on protein's conformation and quaternary structure, thus posing an impact on enzyme activity and thermostability. These results suggest a
Dai S +13 more
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Properties of Thermus aquaticus β‐NADH oxidase immobilised on various supports [PDF]
IUBMB Life, 1997 Abstractβ‐NADH oxidase purified from Thermus aquaticus was covalently immobilised on various solid supports. The preparations obtained were compared with the soluble enzyme for activity and kinetic properties. Activated glutaryl‐PVA was found to be the best support. The immobilised enzyme was less stable at high temperatures than the soluble enzyme. No
Enrico Sanjust +4 more
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Biophysical analysis of Thermus aquaticus single-stranded DNA binding protein. [PDF]
Biophys J, 2008 Due to their involvement in processes such as DNA replication, repair, and recombination, bacterial single-stranded DNA binding (SSB) proteins are essential for the survival of the bacterial cell. Whereas most bacterial SSB proteins form homotetramers in solution, dimeric SSB proteins were recently discovered in the Thermus/Deinococcus group.
Witte G, Fedorov R, Curth U.
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Distinct functions of regions 1.1 and 1.2 of RNA polymerase σ subunits from Escherichia coli and Thermus aquaticus in transcription initiation. [PDF]
J Biol Chem, 2012 Miropolskaya N +5 more
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Modified 'one amino acid-one codon' engineering of high GC content TaqII-coding gene from thermophilic Thermus aquaticus results in radical expression increase. [PDF]
Microb Cell Fact, 2014 BACKGROUND: An industrial approach to protein production demands maximization of cloned gene expression, balanced with the recombinant host’s viability.
Zylicz-Stachula A +4 more
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Anomalous Citrate Synthase from Thermus aquaticus
Journal of General Microbiology, 1978 P.D.J. Weitzman
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