Thermus aquaticus

Related Overviews


'Thermus aquaticus' can also refer to...

Thermus aquaticus

Thermus aquaticus

Thermus aquaticus

Role of Disulphide Bonds in a Thermophilic Serine Protease Aqualysin I from Thermus aquaticus YT-1

Glutamate 83 Is Important for Stabilization of Domain-Domain Conformation of Thermus aquaticus Glycerol Kinase

Investigations on the thermostability and function of truncated Thermus aquaticus DNA polymerase fragments.

Structural studies on an inhibitory antibody against Thermus aquaticus DNA polymerase suggest mode of inhibition.

The crystal structure of the Thermus aquaticus DnaB helicase monomer

Thermodynamics of the binding of Thermus aquaticus DNA polymerase to primed‐template DNA

Domain exchange: chimeras of Thermus aquaticus DNA polymerase, Escherichia coli DNA polymerase I and Thermotoga neapolitana DNA polymerase

RNA polymerase-promoter interactions determining different stability of the Escherichia coli and Thermus aquaticus transcription initiation complexes

Non-homologous recombination mediated by Thermus aquaticus DNA polymerase I. Evidence supporting a copy choice mechanism

Arg660Ser mutation in Thermus aquaticus DNA polymerase I suppresses T→C transitions: implication of wobble base pair formation at the nucleotide incorporation step

UV-induced crosslinks in the 16S rRNAs of Escherichia coli, Bacillus subtilis and Thermus aquaticus and their implications for ribosome structure and photochemistry

Two new thermostable type II restriction endonucleases from Thermus aquaticus: TatI and TauI, which recognize the novel nucleotide sequences 5′-W↓GTACW-3′ and 5′-GCSG↓C-3′ respectively


More Like This

Show all results sharing this subject:

  • Genetics and Genomics


Show Summary Details

Quick Reference

An aerobic, Gram-negative, heterotrophic, thermophilic bacterium discovered in the natural hot springs of Yellowstone National Park, Wyoming. This bacterium became the source of the Taq DNA polymerase used in the polymerase chain reaction (q.v.) and the Taq DNA ligase used in the ligase chain reaction (q.v.). T. aquaticus is also the source of the ribosomes that were used in the crystallographic studies which showed the 3D structure of 70S ribosomes complexed with tRNA and mRNA molecules. See Classification, Bacteria, Deinococci; Chronology, 2001, Yusupov et al.

Subjects: Genetics and Genomics.

Reference entries

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.