title: Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies.
abstract: Antibodies specific for histone post-translational modifications (PTMs) have been central to our understanding of chromatin biology. Here, we describe an unexpected and novel property of histone H4 site-specific acetyl antibodies in that they prefer poly-acetylated histone substrates. By all current criteria, these antibodies have passed specificity standards. However, we find these site-specific histone antibodies preferentially recognize chromatin signatures containing two or more adjacent acetylated lysines. Significantly, we find that the poly-acetylated epitopes these antibodies prefer are evolutionarily conserved and are present at levels that compete for these antibodies over the intended individual acetylation sites. This alarming property of acetyl-specific antibodies has far-reaching implications for data interpretation and may present a challenge for the future study of acetylated histone and non-histone proteins.
authors: Department of Biochemistry & Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
authors: Scott B
authors: SB
authors: Rothbart
authors: Shu
authors: S
authors: Lin
authors: Laura-Mae
authors: LM
authors: Britton
authors: Krzysztof
authors: K
authors: Krajewski
authors: Michael-C
authors: MC
authors: Keogh
authors: Benjamin A
authors: BA
authors: Garcia
authors: Brian D
authors: BD
authors: Strahl
mesh_terms: D000107:Acetylation; D000974:Antibodies, Antinuclear / Q000276:immunology* / Q000378:metabolism; D000918:Antibody Specificity; D042002:Chromatin Assembly and Disassembly; D044127:Epigenesis, Genetic; D000939:Epitopes / Q000737:chemistry / Q000276:immunology*; D006367:HeLa Cells; D006657:Histones / Q000276:immunology* / Q000378:metabolism*; D006801:Humans; D040081:Protein Array Analysis; D011499:Protein Processing, Post-Translational
chemical_list: D000974:Antibodies, Antinuclear; D000939:Epitopes; D006657:Histones