The recognition of specific DNA sequences in processes such as transcription is associated with a cooperative binding of proteins. Some transcription regulation mechanisms involve additional proteins that can influence the binding cooperativity by acting as corepressors or coactivators. In a conditional cooperativity mechanism, the same protein can induce binding cooperativity at one concentration and inhibit it at another. Here, we use calorimetric (ITC) and spectroscopic (UV, CD) experiments to show that such conditional cooperativity can also be achieved by the small DNA-directed oligopeptides distamycin and netropsin. Using a global thermodynamic analysis of the observed binding and (un)folding processes, we calculate the phase diagrams for this system, which show that distamycin binding cooperativity is more pronounced at lower temperatures and can be first induced and then reduced by increasing the netropsin or/and Na+ ion concentration. A molecular interpretation of this phenomenon is suggested.
| Jezik: | Angleški jezik |
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| Ključne besede: | DNA recognition, conditional cooperativity, transcription regulation, protein–DNA interactions, ligand–DNA interactions, distamycin, netropsin, thermodynamics of binding, phase diagrams, DNA folding |
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| Vrsta gradiva: | Članek v reviji |
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| Tipologija: | 1.01 - Izvirni znanstveni članek |
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| Organizacija: | FKKT - Fakulteta za kemijo in kemijsko tehnologijo
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| Status publikacije: | Objavljeno |
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| Različica publikacije: | Objavljena publikacija |
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| Leto izida: | 2021 |
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| Št. strani: | 10 str. |
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| Številčenje: | Vol. 26, iss. 17, art. 5188 |
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| PID: | 20.500.12556/RUL-136078  |
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| UDK: | 577.323 |
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| ISSN pri članku: | 1420-3049 |
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| DOI: | 10.3390/molecules26175188 |
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| COBISS.SI-ID: | 87050755 |
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| Datum objave v RUL: | 11.04.2022 |
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| Število ogledov: | 476 |
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| Število prenosov: | 95 |
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| Metapodatki: |     |
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