title: Molecular basis and specificity of H2A.Z-H2B recognition and deposition by the histone chaperone YL1.
abstract: H2A.Z, a widely conserved histone variant, is evicted from chromatin by the histone chaperone ANP32E. However, to date, no deposition chaperone for H2A.Z is known in metazoans. Here, we identify YL1 as a specific H2A.Z-deposition chaperone. The 2.7-Å-resolution crystal structure of the human YL1-H2A.Z-H2B complex shows that YL1 binding, similarly to ANP32E binding, triggers an extension of the H2A.Z αC helix. The interaction with YL1 is, however, more extensive and includes both the extended acidic patch and the entire DNA-binding surface of H2A.Z-H2B. Substitution of only four amino acid residues of H2A is sufficient for the formation of an H2A.Z-like interface specifically recognized by YL1. Collectively, our data reveal the molecular basis of H2A.Z-specific recognition by YL1 and shed light on the mechanism of H2A.Z transfer to the nucleosome by the ATP-dependent chromatin-remodeling complexes SRCAP and P400-TIP60.
authors.affiliation: Equipe Labélisée Ligue Contre le Cancer, Département de Génomique Fonctionnelle et Cancer, Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
authors.forename: Chrysa M
authors.initials: CM
authors.lastname: Latrick
authors.affiliation: Département de Biologie Structurale Intégrative, IGBMC, Illkirch, France.
authors.forename: Martin
authors.initials: M
authors.lastname: Marek
authors.affiliation: Equipe Labélisée Ligue Contre le Cancer, Département de Génomique Fonctionnelle et Cancer, Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
authors.forename: Khalid
authors.initials: K
authors.lastname: Ouararhni
authors.affiliation: Equipe Labélisée Ligue Contre le Cancer, Département de Génomique Fonctionnelle et Cancer, Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
authors.forename: Christophe
authors.identifier: http://orcid.org/0000-0001-8124-5883
authors.initials: C
authors.lastname: Papin
authors.affiliation: Equipe Labélisée Ligue Contre le Cancer, Département de Génomique Fonctionnelle et Cancer, Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
authors.forename: Isabelle
authors.initials: I
authors.lastname: Stoll
authors.affiliation: Equipe Labélisée Ligue Contre le Cancer, Département de Génomique Fonctionnelle et Cancer, Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
authors.forename: Maria
authors.initials: M
authors.lastname: Ignatyeva
authors.affiliation: Equipe Labélisée Ligue Contre le Cancer, Département de Génomique Fonctionnelle et Cancer, Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
authors.forename: Arnaud
authors.initials: A
authors.lastname: Obri
authors.affiliation: Architecture et Réactivité de l'ARN, Université de Strasbourg, Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg, France.
authors.forename: Eric
authors.initials: E
authors.lastname: Ennifar
authors.affiliation: Département Différenciation et Transformation Cellulaire, Institut Albert Bonniot, Grenoble, France.
authors.forename: Stefan
authors.initials: S
authors.lastname: Dimitrov
authors.affiliation: Département de Biologie Structurale Intégrative, IGBMC, Illkirch, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Romier
authors.affiliation: Equipe Labélisée Ligue Contre le Cancer, Département de Génomique Fonctionnelle et Cancer, Institut de Génétique et Biologie Moléculaire et Cellulaire (IGBMC), Illkirch, France.
authors.forename: Ali
authors.initials: A
authors.lastname: Hamiche
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006367:HeLa Cells; D056488:Histone Chaperones / Q000737:chemistry* / Q000378:metabolism*; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D060066:Protein Interaction Maps; D017433:Protein Structure, Secondary; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D056488:Histone Chaperones; D006657:Histones; D012097:Repressor Proteins; C092773:VPS72 protein, human; C077020:histone H2A.F-Z