title: Effect of temperature on the intrinsic flexibility of DNA and its interaction with architectural proteins.
abstract: 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.
authors.affiliation: Molecular Genetics, Leiden Institute of Chemistry and Cell Observatory, Leiden University , 2333 CC Leiden, The Netherlands.
authors.forename: Rosalie P C
authors.initials: RP
authors.lastname: Driessen
authors.forename: Gerrit
authors.initials: G
authors.lastname: Sitters
authors.forename: Niels
authors.initials: N
authors.lastname: Laurens
authors.forename: Geri F
authors.initials: GF
authors.lastname: Moolenaar
authors.forename: Gijs J L
authors.initials: GJ
authors.lastname: Wuite
authors.forename: Nora
authors.initials: N
authors.lastname: Goosen
authors.forename: Remus Th
authors.initials: RT
authors.lastname: Dame
mesh_terms: D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism*; D042002:Chromatin Assembly and Disassembly; D002868:Chromosomal Proteins, Non-Histone / Q000235:genetics / Q000378:metabolism*; D019641:DNA, Archaeal / Q000737:chemistry* / Q000378:metabolism; D004269:DNA, Bacterial / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D004548:Elasticity; D029968:Escherichia coli Proteins / Q000378:metabolism*; D006358:Hot Temperature; D061925:Immobilized Nucleic Acids / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D009690:Nucleic Acid Conformation; D009691:Nucleic Acid Denaturation; D011994:Recombinant Proteins / Q000378:metabolism; D048229:Sulfolobus solfataricus / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D002868:Chromosomal Proteins, Non-Histone; D019641:DNA, Archaeal; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D061925:Immobilized Nucleic Acids; D011994:Recombinant Proteins; C116822:hns protein, E coli