title: HBO1 HAT complexes target chromatin throughout gene coding regions via multiple PHD finger interactions with histone H3 tail.
abstract: The HBO1 HAT protein is the major source of histone H4 acetylation in vivo and has been shown to play critical roles in gene regulation and DNA replication. A distinctive characteristic of HBO1 HAT complexes is the presence of three PHD finger domains in two different subunits: tumor suppressor proteins ING4/5 and JADE1/2/3. Biochemical and functional analyses indicate that these domains interact with histone H3 N-terminal tail region, but with a different specificity toward its methylation status. Their combinatorial action is essential in regulating chromatin binding and substrate specificity of HBO1 complexes, as well as cell growth. Importantly, localization analyses on the human genome indicate that HBO1 complexes are enriched throughout the coding regions of genes, supporting a role in transcription elongation. These results underline the importance and versatility of PHD finger domains in regulating chromatin association and histone modification crosstalk within a single protein complex.
authors.affiliation: Laval University Cancer Research Center, Hôtel-Dieu de Québec (CHUQ), Quebec City, QC, Canada.
authors.forename: Nehmé
authors.initials: N
authors.lastname: Saksouk
authors.forename: Nikita
authors.initials: N
authors.lastname: Avvakumov
authors.forename: Karen S
authors.initials: KS
authors.lastname: Champagne
authors.forename: Tiffany
authors.initials: T
authors.lastname: Hung
authors.forename: Yannick
authors.initials: Y
authors.lastname: Doyon
authors.forename: Christelle
authors.initials: C
authors.lastname: Cayrou
authors.forename: Eric
authors.initials: E
authors.lastname: Paquet
authors.forename: Mukta
authors.initials: M
authors.lastname: Ullah
authors.forename: Anne-Julie
authors.initials: AJ
authors.lastname: Landry
authors.forename: Valérie
authors.initials: V
authors.lastname: Côté
authors.forename: Xiang-Jiao
authors.initials: XJ
authors.lastname: Yang
authors.forename: Or
authors.initials: O
authors.lastname: Gozani
authors.forename: Tatiana G
authors.initials: TG
authors.lastname: Kutateladze
authors.forename: Jacques
authors.initials: J
authors.lastname: Côté
mesh_terms: D000107:Acetylation; D001665:Binding Sites; D002478:Cells, Cultured; D002843:Chromatin / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D006367:HeLa Cells; D051548:Histone Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D018398:Homeodomain Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008745:Methylation; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism
chemical_list: D002843:Chromatin; D004268:DNA-Binding Proteins; D006657:Histones; D018398:Homeodomain Proteins; D051548:Histone Acetyltransferases