title: Histone H3 tails containing dimethylated lysine and adjacent phosphorylated serine modifications adopt a specific conformation during mitosis and meiosis.
abstract: Condensation of chromatin, mediated in part by posttranslational modifications of histones, is essential for cell division during mitosis. Histone H3 tails are dimethylated on lysine (Kme2) and become phosphorylated on serine (Sp) residues during mitosis. We have explored the possibility that these double modifications are involved in the establishment of H3 tail conformations during the cell cycle. Here we describe a specific chromatin conformation occurring at Kme2 and adjacently phosphorylated S of H3 tails upon formation of a hydrogen bond. This conformation appears exclusively between early prophase and early anaphase of the mitosis, when chromatin condensation is highest. Moreover, we observed that the conformed H3Kme2Sp tail is present at the diplotene and metaphase stages in spermatocytes and oocytes. Our data together with results obtained by cryoelectron microscopy suggest that the conformation of Kme2Sp-modified H3 tails changes during mitosis and meiosis. This is supported by biostructural modeling of a modified histone H3 tail bound by an antibody, indicating that Kme2Sp-modified H3 tails can adopt at least two different conformations. Thus, the H3K9me2S10p and the H3K27me2S28p sites are involved in the acquisition of specific chromatin conformations during chromatin condensation for cell division.
authors.affiliation: Institut de Génétique et de Biologie Moléculaire et Cellulaire, INSERM, U.596, CNRS-LGME, ULP, Parc d'Innovation, 1, rue Laurent Fries, BP 10142, Illkirch Cedex, CU de Strasbourg 67404, France.
authors.forename: Adrien
authors.initials: A
authors.lastname: Eberlin
authors.forename: Cédric
authors.initials: C
authors.lastname: Grauffel
authors.forename: Mustapha
authors.initials: M
authors.lastname: Oulad-Abdelghani
authors.forename: Flavie
authors.initials: F
authors.lastname: Robert
authors.forename: Maria-Elena
authors.initials: ME
authors.lastname: Torres-Padilla
authors.forename: Romain
authors.initials: R
authors.lastname: Lambrot
authors.forename: Danièle
authors.initials: D
authors.lastname: Spehner
authors.forename: Lourdes
authors.initials: L
authors.lastname: Ponce-Perez
authors.forename: Jean-Marie
authors.initials: JM
authors.lastname: Würtz
authors.forename: Roland H
authors.initials: RH
authors.lastname: Stote
authors.forename: Sarah
authors.initials: S
authors.lastname: Kimmins
authors.forename: Patrick
authors.initials: P
authors.lastname: Schultz
authors.forename: Annick
authors.initials: A
authors.lastname: Dejaegere
authors.forename: Laszlo
authors.initials: L
authors.lastname: Tora
mesh_terms: D000818:Animals; D006690:Bisbenzimidazole / Q000378:metabolism; D005260:Female; D005456:Fluorescent Dyes / Q000378:metabolism; D006367:HeLa Cells; D006657:Histones / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D006860:Hydrogen Bonding; D008239:Lysine / Q000378:metabolism; D008297:Male; D008540:Meiosis; D008745:Methylation; D051379:Mice; D008815:Mice, Inbred Strains; D008938:Mitosis; D041681:NIH 3T3 Cells; D009865:Oocytes / Q000378:metabolism / Q000648:ultrastructure; D010766:Phosphorylation; D011487:Protein Conformation; D012694:Serine / Q000378:metabolism; D013737:Testis / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D005456:Fluorescent Dyes; D006657:Histones; D012694:Serine; D008239:Lysine; D006690:Bisbenzimidazole