title: Scratching the (lateral) surface of chromatin regulation by histone modifications.
abstract: Histones have two structurally and functionally distinct domains: globular domains forming the nucleosomal core around which DNA is wrapped and unstructured tails protruding from the nucleosomal core. Whereas post-translational modifications (PTMs) in histone tails are well studied, much less is currently known about histone-core PTMs. Many core PTMs map to residues located on the lateral surface of the histone octamer, close to the DNA, and they have the potential to alter intranucleosomal histone-DNA interactions. Here we discuss recent advances in understanding the function of lateral-surface PTMs. Whereas modifications in the histone tails might have limited structural impact on the nucleosome itself and function as signals to recruit specific binding proteins, PTMs in the lateral surface can have a direct structural effect on nucleosome and chromatin dynamics, even in the absence of specific binding proteins, which adds a twist to the debate on the functionality and causality of PTMs.
authors.affiliation: Max Planck Institute of Immunobiology and Epigenetics, Freiburg, Germany.
authors.forename: Philipp
authors.initials: P
authors.lastname: Tropberger
authors.forename: Robert
authors.initials: R
authors.lastname: Schneider
mesh_terms: D002843:Chromatin / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D009707:Nucleosomes / Q000378:metabolism; D011485:Protein Binding; D011499:Protein Processing, Post-Translational
chemical_list: D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D004247:DNA