Cargando…
Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies
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...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3388470/ https://www.ncbi.nlm.nih.gov/pubmed/22761995 http://dx.doi.org/10.1038/srep00489 |
_version_ | 1782237196795772928 |
---|---|
author | Rothbart, Scott B. Lin, Shu Britton, Laura-Mae Krajewski, Krzysztof Keogh, Michael-C Garcia, Benjamin A. Strahl, Brian D. |
author_facet | Rothbart, Scott B. Lin, Shu Britton, Laura-Mae Krajewski, Krzysztof Keogh, Michael-C Garcia, Benjamin A. Strahl, Brian D. |
author_sort | Rothbart, Scott B. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3388470 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-33884702012-07-03 Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies Rothbart, Scott B. Lin, Shu Britton, Laura-Mae Krajewski, Krzysztof Keogh, Michael-C Garcia, Benjamin A. Strahl, Brian D. Sci Rep Article 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. Nature Publishing Group 2012-07-03 /pmc/articles/PMC3388470/ /pubmed/22761995 http://dx.doi.org/10.1038/srep00489 Text en Copyright © 2012, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareALike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ |
spellingShingle | Article Rothbart, Scott B. Lin, Shu Britton, Laura-Mae Krajewski, Krzysztof Keogh, Michael-C Garcia, Benjamin A. Strahl, Brian D. Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies |
title | Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies |
title_full | Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies |
title_fullStr | Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies |
title_full_unstemmed | Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies |
title_short | Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies |
title_sort | poly-acetylated chromatin signatures are preferred epitopes for site-specific histone h4 acetyl antibodies |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3388470/ https://www.ncbi.nlm.nih.gov/pubmed/22761995 http://dx.doi.org/10.1038/srep00489 |
work_keys_str_mv | AT rothbartscottb polyacetylatedchromatinsignaturesarepreferredepitopesforsitespecifichistoneh4acetylantibodies AT linshu polyacetylatedchromatinsignaturesarepreferredepitopesforsitespecifichistoneh4acetylantibodies AT brittonlauramae polyacetylatedchromatinsignaturesarepreferredepitopesforsitespecifichistoneh4acetylantibodies AT krajewskikrzysztof polyacetylatedchromatinsignaturesarepreferredepitopesforsitespecifichistoneh4acetylantibodies AT keoghmichaelc polyacetylatedchromatinsignaturesarepreferredepitopesforsitespecifichistoneh4acetylantibodies AT garciabenjamina polyacetylatedchromatinsignaturesarepreferredepitopesforsitespecifichistoneh4acetylantibodies AT strahlbriand polyacetylatedchromatinsignaturesarepreferredepitopesforsitespecifichistoneh4acetylantibodies |