title: A brief histone in time: understanding the combinatorial functions of histone PTMs in the nucleosome context.
abstract: It has been over 50 years since Allfrey et al. proposed that histone acetylation regulates RNA synthesis, and the study of histone modifications has progressed at an extraordinary pace for the past two decades. In this review, we provide a perspective on some key events and advances in our understanding of histone modifications. We also highlight reagents and tools from past to present that facilitated progress in this research field. Using histone H3 phosphorylation as an underlying thread, we review the rationale that led to the proposal of the histone code hypothesis, as well as examples that illustrate the concepts of combinatorial histone modifications and cross-talk pathways. We further highlight the importance of investigating these mechanisms in the context of nucleosomes rather than just at the histone level and present current and developing approaches for such studies. Overall, research on histone modifications has yielded great mechanistic insights into the regulation of genomic functions, and extending these studies using nucleosomes will further elucidate the complexity of these pathways in a more physiologically relevant context.
authors.affiliation: Department of Biology, York University, Life Sciences Building, Rm 331A, Toronto, ON M3J 1P3, Canada.|Department of Biology, York University, Life Sciences Building, Rm 331A, Toronto, ON M3J 1P3, Canada.
authors.forename: Marlee K
authors.initials: MK
authors.lastname: Ng
authors.affiliation: Department of Biology, York University, Life Sciences Building, Rm 331A, Toronto, ON M3J 1P3, Canada.|Department of Biology, York University, Life Sciences Building, Rm 331A, Toronto, ON M3J 1P3, Canada.
authors.forename: Peter
authors.initials: P
authors.lastname: Cheung
mesh_terms: D000107:Acetylation; D002843:Chromatin / Q000378:metabolism*; D044127:Epigenesis, Genetic; D051548:Histone Acetyltransferases / Q000378:metabolism*; D042421:Histone Code; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D008745:Methylation; D009707:Nucleosomes / Q000378:metabolism*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism
chemical_list: D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D011495:Histone-Lysine N-Methyltransferase; D051548:Histone Acetyltransferases; D017346:Protein Serine-Threonine Kinases
keywords: chromatin; chromatine; epigenetics; histone modification; modification des histones; multivalence; multivalency; nucleosome; nucléosome; épigénétique