Nucleosome conformational flexibility and implications for chromatin dynamics

• Published in: Philosophical transactions of the Royal Society of London. Series A: Mathematical, physical, and engineering sciences Vol. 362; no. 1820; pp. 1519 - 1547
• Main Authors: Sivolob, Andrei, Prunell, Ariel
• Format: Journal Article
• Language: English
• Published: England The Royal Society 15.07.2004
• Subjects: Acetylation; Base Sequence; Biological Structures; Chromatin; Chromatin - chemistry; Conformational Flexibility; Dimers; DNA; DNA - chemistry; DNA - ultrastructure; Dna Supercoiling; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - ultrastructure; Dyadic relations; Elasticity; Genetic equilibrium; Histones; Models, Molecular; Molecular Sequence Data; Motion; Nucleic Acid Conformation; Nucleic Acid Denaturation; Nucleosome; Nucleosomes; Nucleosomes - chemistry; Nucleosomes - ultrastructure; Periodicity; Stress, Mechanical; Structure-Activity Relationship; Topology; Torque
• ISSN: 1364-503X; 1471-2962
• DOI: 10.1098/rsta.2004.1387

histone tetramer–containing particle, now known as the tetrasome; the nucleosome; and the linker histone H5/H1–bearing nucleosome (the chromatosome). All the particles were found to exist in two to three conformational states, which differ by their topological and mechanical properties. Our approach unveiled the molecular mechanisms of nucleosome conformational dynamics and will help to understand its functional relevance. A most surprising conclusion of the work was perhaps that DNA overall flexibility
considerably upon particle formation, which might indeed be a requirement of genome function.
The active role of chromatin in the regulation of gene activity seems to imply a conformational flexibility of the basic chromatin structural unit, the nucleosome. This review is devoted to our recent results pertaining to this subject, using an original approach based on the topology of single particles reconstituted on DNA minicircles, combined with their theoretical simulation. Three types of chromatin particles have been studied so far: a subnucleosome, that is, the (H3–H4)