Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer
| Autor: | Sumedha Jayasena, Yun Lin |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Hot Temperature
DNA polymerase Macromolecular Substances Aptamer Molecular Sequence Data DNA-Directed DNA Polymerase Polymerase Chain Reaction Substrate Specificity chemistry.chemical_compound Structural Biology Enzyme Stability Taq Polymerase Thermus Molecular Biology Polymerase Nucleic Acid Synthesis Inhibitors biology Base Sequence Thermus thermophilus biology.organism_classification Molecular biology Kinetics chemistry Oligodeoxyribonucleotides biology.protein Nucleic Acid Conformation Thermodynamics Dimerization Systematic evolution of ligands by exponential enrichment Hot start PCR Taq polymerase |
| Zdroj: | Journal of molecular biology. 271(1) |
| ISSN: | 0022-2836 |
| Popis: | Single-stranded DNA aptamers that recognize DNA polymerase from Thermus acquaticus (Taq pol) with high affinity have been described recently. These aptamers have been shown to efficiently inhibit the polymerase activity of Taq pol and are useful in enhancing the amplification efficiency of low copy number targets by the polymerase chain reaction (PCR). Aptamers selected to bind to Taq pol fell into two different sequence families and inhibited several DNA polymerases isolated from the Thermus species, including that from Thermus thermophilus (Tth pol). Aptamers from one sequence family inhibited the Stoffel fragment of Taq pol efficiently, whereas those from the other family did not. Truncated aptamers derived from two parent ligands from both families were combined to form a heterodimeric aptamer that effectively inhibited all three polymerases and were shown to be useful in detecting a low copy number target by PCR amplification. These data demonstrate that the combination of aptamers with different properties into a single molecule broadens their spectrum of utility. |
| Databáze: | OpenAIRE |
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