3QZS

Crystal Structure of BPTF bromo in complex with histone H4K16ac - Form I

Summary for 3QZS

• Entry DOI: 10.2210/pdb3qzs/pdb
• Related: 3QZT 3QZV
• Descriptor: Nucleosome-remodeling factor subunit BPTF, Histone H4 (3 entities in total)
• Functional Keywords: protein-peptide complex, transcription-nuclear protein complex, transcription/nuclear protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q12830; Nucleus: P62805
• Total number of polymer chains: 4
• Total formula weight: 29137.33

Authors

Li, H.,Ruthenburg, A.J.,Patel, D.J. (deposition date: 2011-03-07, release date: 2011-06-01, Last modification date: 2024-11-20)

Primary citation

Ruthenburg, A.J.,Li, H.,Milne, T.A.,Dewell, S.,McGinty, R.K.,Yuen, M.,Ueberheide, B.,Dou, Y.,Muir, T.W.,Patel, D.J.,Allis, C.D.
Recognition of a Mononucleosomal Histone Modification Pattern by BPTF via Multivalent Interactions.
Cell(Cambridge,Mass.), 145:692-706, 2011

PubMed Abstract: Little is known about how combinations of histone marks are interpreted at the level of nucleosomes. The second PHD finger of human BPTF is known to specifically recognize histone H3 when methylated on lysine 4 (H3K4me2/3). Here, we examine how additional heterotypic modifications influence BPTF binding. Using peptide surrogates, three acetyllysine ligands are indentified for a PHD-adjacent bromodomain in BPTF via systematic screening and biophysical characterization. Although the bromodomain displays limited discrimination among the three possible acetyllysines at the peptide level, marked selectivity is observed for only one of these sites, H4K16ac, in combination with H3K4me3 at the mononucleosome level. In support, these two histone marks constitute a unique trans-histone modification pattern that unambiguously resides within a single nucleosomal unit in human cells, and this module colocalizes with these marks in the genome. Together, our data call attention to nucleosomal patterning of covalent marks in dictating critical chromatin associations.

PubMed: 21596426
DOI: 10.1016/j.cell.2011.03.053

Experimental method

X-RAY DIFFRACTION (1.8 Å)