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H3 and H4 Histone Tails Play a Central Role in the Interactions of Recombinant NCPs

Aurélie Bertin ^* , Madalena Renouard ^*, Jan Skov Pedersen , Françoise Livolant ^* and Dominique Durand 

^* Laboratoire de Physique des Solides, Centre National de la Recherche Scientifique, UMR 8502, Université Paris-Sud, 91405 Orsay Cédex, France; Department of Chemistry and iNANO Interdisciplinary Nanoscience Centre, University of Aarhus, Aarhus, Denmark; Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, UMR 8619, Université Paris Sud, 91405 Orsay Cédex, France; and Molecular and Cellular Biology Department, University of California, Berkeley, California 94720-3200

Correspondence: Address reprint requests to A. Bertin, E-mail: bertin{at}berkeley.edu; or D. Durand, e-mail: dominique.durand{at}u-psud.fr.

Using small-angle x-ray scattering, we probe the effect of histone tails on both internucleosomal interactions and nucleosome conformation. To get insight into the specific role of H3 and H4 histone tails, perfectly monodisperse recombinant nucleosome core particles were reconstituted, either intact or deprived of both H3 and H4 histone tails (gH3gH4). The main result is that H3 and H4 histone tails are necessary to induce attractive interactions between NCPs. A pair potential model was used to describe interactions between NCPs. At all salt concentrations, interactions between gH3gH4 NCPs are best described by repulsive interactions exclusively. For intact NCPs, an additional attractive term, with a 5–10 kT magnitude and 20 Å range, is required to account for interparticle interactions above 50 mM monovalent salt. Regarding conformation, intact NCPs in solution are similar to NCPs in 3D crystals. gH3gH4 NCPs instead give rise to slightly different small-angle x-ray scattering curves that can be understood as a more opened conformation of the particle, where DNA ends are slightly detached from the core.