Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions Journal Article

   

Authors:	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.
Article Title:	Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions
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. © 2011 Elsevier Inc.
Journal Title:	Cell
Volume:	145
Issue:	5
ISSN:	0092-8674
Publisher:	Cell Press
Date Published:	2011-05-27
Start Page:	692
End Page:	706
Language:	English
DOI:	10.1016/j.cell.2011.03.053
PROVIDER:	scopus
PUBMED:	21596426
PMCID:	PMC3135172
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-79957537645&partnerID=40&md5=df0f116c572fcf4bf23376855cddeb9f
Notes:	--- - "Export Date: 23 June 2011" - "CODEN: CELLB" - "Source: Scopus"

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