title: Solution structure and NMR characterization of the binding to methylated histone tails of the plant homeodomain finger of the tumour suppressor ING4.
abstract: Plant homeodomain (PHD) fingers are frequently present in proteins involved in chromatin remodelling, and some of them bind to histones. The family of proteins inhibitors of growth (ING) contains a PHD finger that bind to histone-3 trimethylated at lysine 4, and those of ING1 and ING2 also act as nuclear phosphoinositide receptors. We have determined the structure of ING4 PHD, and characterised its binding to phosphoinositides and histone methylated tails. In contrast to ING2, ING4 is not a phosphoinositide receptor and binds with similar affinity to the different methylation states of histone-3 at lysine 4.
authors.affiliation: NMR Group, Centro Nacional de Investigaciones Oncológicas (CNIO), Melchor Fernández Almagro 3, 28029 Madrid, Spain.
authors.forename: Alicia
authors.initials: A
authors.lastname: Palacios
authors.forename: Pascal
authors.initials: P
authors.lastname: Garcia
authors.forename: Daniel
authors.initials: D
authors.lastname: Padró
authors.forename: Eva
authors.initials: E
authors.lastname: López-Hernández
authors.forename: Irene
authors.initials: I
authors.lastname: Martín
authors.forename: Francisco J
authors.initials: FJ
authors.lastname: Blanco
mesh_terms: D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D018398:Homeodomain Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008745:Methylation; D008958:Models, Molecular; D009154:Mutation / Q000235:genetics; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D025521:Tumor Suppressor Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D006657:Histones; D018398:Homeodomain Proteins; D025521:Tumor Suppressor Proteins