Results 1 to 10 of about 24,101 (229)

Complete Genome Sequence of Thermus aquaticus Y51MC23. [PDF]

open access: yesPLoS ONE, 2015
Thermus aquaticus Y51MC23 was isolated from a boiling spring in the Lower Geyser Basin of Yellowstone National Park. Remarkably, this T. aquaticus strain is able to grow anaerobically and produces multiple morphological forms. Y51MC23 is a Gram-negative,
Phillip J Brumm   +7 more
doaj   +7 more sources

A robust strategy for overexpression of DNA polymerase from Thermus aquaticus using an IPTG-independent autoinduction system in a benchtop bioreactor [PDF]

open access: goldScientific Reports
The DNA polymerase derived from Thermus aquaticus is the most widely utilized among various DNA polymerases, indicating its significant economic importance. Consequently, efforts to achieve a substantial yield of Taq DNA polymerase (Taq-pol) are ongoing.
Fina Amreta Laksmi   +11 more
doaj   +4 more sources

Crystal structure of a Thermus aquaticus diversity-generating retroelement variable protein. [PDF]

open access: yesPLoS ONE, 2019
Diversity-generating retroelements (DGRs) are widely distributed in bacteria, archaea, and microbial viruses, and bring about unparalleled levels of sequence variation in target proteins.
Sumit Handa   +2 more
doaj   +3 more sources

Variants of a Thermus aquaticus DNA polymerase with increased selectivity for applications in allele- and methylation-specific amplification. [PDF]

open access: yesPLoS ONE, 2014
The selectivity of DNA polymerases is crucial for many applications. For example, high discrimination between the extension of matched versus mismatched primer termini is desired for the detection of a single nucleotide variation at a particular locus ...
Matthias Drum   +4 more
doaj   +3 more sources

Inhibitory Effect of Bridged Nucleosides on Thermus aquaticus DNA Polymerase and Insight into the Binding Interactions. [PDF]

open access: yesPLoS ONE, 2016
Modified nucleosides have the potential to inhibit DNA polymerases for the treatment of viral infections and cancer. With the hope of developing potent drug candidates by the modification of the 2',4'-position of the ribose with the inclusion of a bridge,
Sung-Kun Kim   +5 more
doaj   +3 more sources

Modified 'one amino acid-one codon' engineering of high GC content TaqII-coding gene from thermophilic Thermus aquaticus results in radical expression increase. [PDF]

open access: yesMicrob 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
europepmc   +3 more sources

Distinct functions of regions 1.1 and 1.2 of RNA polymerase σ subunits from Escherichia coli and Thermus aquaticus in transcription initiation. [PDF]

open access: hybridJ Biol Chem, 2012
Background: RNA polymerases (RNAPs) from Thermus aquaticus and Escherichia coli differ in many aspects of transcription initiation. Results: Regions 1.1 and 1.2 of the σ subunit determine instability and cold sensitivity of promoter complexes of T ...
Miropolskaya N   +5 more
europepmc   +4 more sources

Incorporation of N7-Platinated Guanines into Thermus Aquaticus (Taq) DNA Polymerase: Atomistic Insights from Molecular Dynamics Simulations. [PDF]

open access: yesInt J Mol Sci, 2023
In this work, we elucidated some key aspects of the mechanism of action of the cisplatin anticancer drug, cis-[Pt(NH3)2Cl2], involving direct interactions with free nucleotides.
De Castro F   +5 more
europepmc   +2 more sources

Identification of Thermus aquaticus DNA polymerase variants with increased mismatch discrimination and reverse transcriptase activity from a smart enzyme mutant library. [PDF]

open access: yesSci Rep, 2019
DNA polymerases the key enzymes for several biotechnological applications. Obviously, nature has not evolved these enzymes to be compatible with applications in biotechnology. Thus, engineering of a natural scaffold of DNA polymerases may lead to enzymes
Raghunathan G, Marx A.
europepmc   +2 more sources

The third restriction-modification system from Thermus aquaticus YT-1: solving the riddle of two TaqII specificities. [PDF]

open access: yesNucleic Acids Res, 2017
Two restriction–modification systems have been previously discovered in Thermus aquaticus YT-1. TaqI is a 263-amino acid (aa) Type IIP restriction enzyme that recognizes and cleaves within the symmetric sequence 5′-TCGA-3′.
Skowron PM   +13 more
europepmc   +2 more sources

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