@article {2018|2094,
	title = {Holding the Nucleosome Together: A Quantitative Description of the DNA-Histone Interface in Solution.},
	journal = {J Chem Theory Comput},
	volume = {14},
	year = {2018},
	month = {2018 Feb 13},
	pages = {1045-1058},
	abstract = {<p>The nucleosome is the fundamental unit of eukaryotic genome packaging in the chromatin. In this complex, the DNA wraps around eight histone proteins to form a superhelical double helix. The resulting bending, stronger than anything observed in free DNA, raises the question of how such a distortion is stabilized by the proteic and solvent environments. In this work, the DNA-histone interface in solution was exhaustively analyzed from nucleosome structures generated by molecular dynamics. An original Voronoi tessellation technique, measuring the topology of interacting elements without any empirical or subjective adjustment, was used to characterize the interface in terms of contact area and occurrence. Our results revealed an interface more robust than previously known, combining extensive, long-lived nonelectrostatic and electrostatic interactions between DNA and both structured and unstructured histone regions. Cation accumulation makes the proximity of juxtaposed DNA gyres in the superhelix possible by shielding the strong electrostatic repulsion of the charged phosphate groups. Overall, this study provides new insights on the nucleosome cohesion, explaining how DNA distortions can be maintained in a nucleoprotein complex.</p>
},
	keywords = {DNA, Histones, Molecular Dynamics Simulation, Nucleosomes, Solutions, Static Electricity},
	issn = {1549-9626},
	doi = {10.1021/acs.jctc.7b00936},
	author = {Elbahnsi, Ahmad and Retureau, Romain and Marc Baaden and Hartmann, Brigitte and Oguey, Christophe}
}
@article {2005|1775,
	title = {Chromatin remodeling complexes: ATP-dependent machines in action.},
	journal = {Biochem. Cell Biol.},
	volume = {83},
	number = {4},
	year = {2005},
	month = {aug},
	pages = {405{\textendash}417},
	publisher = {Division of Biological Sciences, Marshall University, Huntington, WV 25755, USA.},
	abstract = {Since the initial characterization of chromatin remodeling as an ATP-dependent process, many studies have given us insight into how nucleosome-remodeling complexes can affect various nuclear functions. However, the multistep DNA-histone remodeling process has not been completely elucidated. Although new studies are published on a nearly weekly basis, the nature and roles of interactions of the individual SWI/SNF- and ISWI-based remodeling complexes and DNA, core histones, and other chromatin-associated proteins are not fully understood. In addition, the potential changes associated with ATP recruitment and its subsequent hydrolysis have not been fully characterized. This review explores possible mechanisms by which chromatin-remodeling complexes are recruited to specific loci, use ATP hydrolysis to achieve actual remodeling through disruption of DNA-histone interactions, and are released from their chromatin template. We propose possible roles for ATP hydrolysis in a chromatin-release/target-scanning process that offer an alternative to or complement the often overlooked function of delivering the energy required for sliding or dislodging specific subsets of core histones.},
	keywords = {Adenosine Triphosphatases, Adenosine Triphosphate, Animals, Chromatin, Gene Expression Regulation, genetics/metabolism, Humans, metabolism, Nucleosomes, Transcription Factors},
	doi = {10.1139/o05-115},
	author = {Cotteka N Johnson and Nicholas L Adkins and Philippe Georgel}
}
