Downstream Oligonucleotides Strongly Enhance the Affinity of GMP to RNA Primer–Template Complexes
| Autor: | Enver Cagri Izgu, Noam Prywes, Anders Björkbom, Chun Pong Tam, Albert C. Fahrenbach, Jack W. Szostak |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Guanosine Monophosphate Oligonucleotides Guanosine 010402 general chemistry 01 natural sciences Biochemistry Catalysis 03 medical and health sciences chemistry.chemical_compound Viral Proteins Colloid and Surface Chemistry Downstream (manufacturing) Binding site Binding Sites Oligonucleotide GMP binding Communication RNA General Chemistry DNA-Directed RNA Polymerases Orders of magnitude (mass) 0104 chemical sciences 030104 developmental biology Monomer chemistry Thermodynamics |
| Zdroj: | Journal of the American Chemical Society |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | Origins of life hypotheses often invoke a transitional phase of nonenzymatic template-directed RNA replication prior to the emergence of ribozyme-catalyzed copying of genetic information. Here, using NMR and ITC, we interrogate the binding affinity of guanosine 5′-monophosphate (GMP) for primer–template complexes when either another GMP, or a helper oligonucleotide, can bind downstream. Binding of GMP to a primer–template complex cannot be significantly enhanced by the possibility of downstream monomer binding, because the affinity of the downstream monomer is weaker than that of the first monomer. Strikingly, GMP binding affinity can be enhanced by ca. 2 orders of magnitude when a helper oligonucleotide is stably bound downstream of the monomer binding site. We compare these thermodynamic parameters to those previously reported for T7 RNA polymerase-mediated replication to help address questions of binding affinity in related nonenzymatic processes. |
| Databáze: | OpenAIRE |
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