We use the wormlike chain model to study supercoiling of DNA under tension and torque. The model reproduces experimental data for a broad range of forces, salt concentrations, and contour lengths. We find a plane of first-order phase transitions ending in a smeared-out line of critical points, the multiplectoneme phase, which is characterized by a fast twist-mediated diffusion of plectonemes and a torque that rises after plectoneme formation with increasing linking number. The discovery of this phase at the same time resolves the discrepancies between existing models and experiment.

Archaeal chromatin proteins share molecular and functional similarities with both bacterial and eukaryotic chromatin proteins. These proteins play an important role in functionally organizing the genomic DNA into a compact nucleoid. Cren7 and Sul7 are two crenarchaeal nucleoid-associated proteins, which are structurally homologous, but not conserved at the sequence level. Co-crystal structures have shown that these two proteins induce a sharp bend on binding to DNA. In this study, we have investigated the architectural properties of these proteins using atomic force microscopy, molecular dynamics simulations and magnetic tweezers. We demonstrate that Cren7 and Sul7 both compact DNA molecules to a similar extent. Using a theoretical model, we quantify the number of individual proteins bound to the DNA as a function of protein concentration and show that forces up to 3.5 pN do not affect this binding. Moreover, we investigate the flexibility of the bending angle induced by Cren7 and Sul7 and show that the protein–DNA complexes differ in flexibility from analogous bacterial and eukaryotic DNA-bending proteins.

We present a model that predicts the geometry of chromatin fibers as a function of the DNA repeat length. Chromatin fibers are widely observed in vitro and are typically posited as the second level of the hierarchical organization of chromatin in the nuclei of cells. We postulate that the major driving force for fiber formation is the dense packing of the underlying DNAprotein spools, the nucleosomes, allowing for fibers with four possible diameters. We show that the diameters observed in experiments on reconstituted regular fibers correspond to the geometries that minimize the elastic energy of the DNA linking the nucleosomes.