Effect of Temperature on the Intrinsic Flexibility of DNA and Its Interaction with Architectural Proteins
| Autor: | Gerrit Sitters, Niels Laurens, Geri F. Moolenaar, Remus T. Dame, Gijs J.L. Wuite, Nora Goosen, Rosalie P. C. Driessen |
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| Přispěvatelé: | Physics of Living Systems, LaserLaB - Molecular Biophysics, Neuroscience Campus Amsterdam - Brain Imaging Technology |
| Rok vydání: | 2014 |
| Předmět: |
DNA
Bacterial Hot Temperature Chromosomal Proteins Non-Histone Archaeal Proteins Immobilized Nucleic Acids Plasma protein binding Biology Nucleic Acid Denaturation Models Biological Biochemistry Temperature measurement Article chemistry.chemical_compound Genomic organization Escherichia coli Proteins Chromatin Assembly and Disassembly Elasticity Recombinant Proteins Chromatin DNA-Binding Proteins Crystallography DNA Archaeal Tethered particle motion chemistry 13. Climate action Sulfolobus solfataricus Biophysics Nucleic Acid Conformation DNA |
| Zdroj: | Biochemistry Driessen, R P C, Sitter, G, Moolenaar, G F, Wuite, G J L, Goosen, N & Dame, R T 2014, ' Effect of Temperature on the Intrinsic Flexibility of DNA and Its Interaction with Architectural Proteins ', Biochemistry, vol. 2014, no. 53, pp. 6430-6438 . https://doi.org/10.1021/bi500344j Biochemistry, 2014(53), 6430-6438. American Chemical Society |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi500344j |
| Popis: | The helical structure of double-stranded DNA is destabilized by increasing temperature. Above a critical temperature (the melting temperature), the two strands in duplex DNA become fully separated. Below this temperature, the structural effects are localized. Using tethered particle motion in a temperature-controlled sample chamber, we systematically investigated the effect of increasing temperature on DNA structure and the interplay between this effect and protein binding. Our measurements revealed that (1) increasing temperature enhances DNA flexibility, effectively leading to more compact folding of the double-stranded DNA chain, and (2) temperature differentially affects different types of DNA-bending chromatin proteins from mesophilic and thermophilic organisms. Thus, our findings aid in understanding genome organization in organisms thriving at moderate as well as extreme temperatures. Moreover, our results underscore the importance of carefully controlling and measuring temperature in single-molecule DNA (micromanipulation) experiments. |
| Databáze: | OpenAIRE |
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