Nucleosome gaping supports a functional structure for the 30nm chromatin fiber.
The biological functions played by the nucleus of eukaryotic cells and especially those involved in cellular differentiation not only depend on the genomic sequence but also on all the proteins which form the nucleo-protein complex named chromatin. The tridimensional organization of this huge polymer involves many structural levels, the most basic one being the nucleosome. Nucleosomes further organize into the so-called 30nm fiber, which, according to recent works, is likely to be the main functional level of chromatin. We wish here to propose a plausible structure for the 30nm chromatin fiber that could explain its functional role. In our model, silenced chromatin is locked by nucleosome stacking interactions. This is achieved by a conformational transition within the nucleosome core particle (NCP) which allows nucleosomes to stack along two helices without bending the DNA linkers. We used molecular modeling to check that this conformational transition was plausible. Then we proposed to modify the well-known two-angle model according to these atomic level results. The emerging picture is an allosteric behavior of the nucleosomes induced by their collective organization within the 30nm chromatin fiber.
Mozziconacci
Julien
J
Laboratoire de Physique Theorique des Liquides, CNRS UMR 7600, Universite Pierre et Marie Curie, Case Courrier 121, 4 place Jussieu, 75252 Paris Cedex 05, France.
Victor
Jean-Marc
JM
D000465:Algorithms; D000495:Allosteric Site; D000818:Animals; D002843:Chromatin / Q000737:chemistry*; D004247:DNA / Q000737:chemistry; D004220:Disulfides; D005786:Gene Expression Regulation; D006657:Histones / Q000737:chemistry; D008958:Models, Molecular; D008962:Models, Theoretical; D008968:Molecular Conformation; D009707:Nucleosomes / Q000737:chemistry*; D017433:Protein Structure, Secondary
D002843:Chromatin; D004220:Disulfides; D006657:Histones; D009707:Nucleosomes; D004247:DNA