The organization of histone H3 modifications as revealed by a panel of specific monoclonal antibodies
- PMID: 18227620
- DOI: 10.1247/csf.07035
The organization of histone H3 modifications as revealed by a panel of specific monoclonal antibodies
Abstract
Histone modifications play critical roles in the epigenetic regulation of gene expression and in the maintenance of genome integrity. Acetylation and methylation of histone H3 are particularly important in gene activation and silencing. We generated and characterized a panel of mouse monoclonal antibodies that specifically recognize different modifications on K4, K9, and K27 residues on histone H3. By using these antibodies for chromatin immunoprecipitation and immunoblotting, we analyzed the relationship between different modifications in nearby nucleosomes in human cells. Within a few nucleosome neighbors, trimethyl-K4 was associated with acetyl-K27, rather than with dimethyl-K4 and acetyl-K9, consistent with their co-localization on active promoters. Furthermore, simultaneous immunofluorescence using directly-labeled antibodies revealed that di- and tri-methylation on K4 was diminished during replicative senescence. These highly-reliable and fully-characterized monoclonal antibodies may facilitate future epigenomic studies on healthy and diseased cells.
Similar articles
-
Structural cooperativity in histone H3 tail modifications.Protein Sci. 2011 Dec;20(12):1982-90. doi: 10.1002/pro.745. Epub 2011 Oct 19. Protein Sci. 2011. PMID: 21956975 Free PMC article.
-
Histone H3 acetylation and H3 K4 methylation define distinct chromatin regions permissive for transgene expression.Mol Cell Biol. 2006 Sep;26(17):6357-71. doi: 10.1128/MCB.00311-06. Mol Cell Biol. 2006. PMID: 16914722 Free PMC article.
-
Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase.Mol Cell. 2001 Dec;8(6):1207-17. doi: 10.1016/s1097-2765(01)00405-1. Mol Cell. 2001. PMID: 11779497
-
[The roles of histone lysine methylation in epigenetic regulation].Yi Chuan. 2007 Apr;29(4):387-92. doi: 10.1360/yc-007-0387. Yi Chuan. 2007. PMID: 17548299 Review. Chinese.
-
Histone methyltransferases: novel targets for tumor and developmental defects.Am J Transl Res. 2015 Nov 15;7(11):2159-75. eCollection 2015. Am J Transl Res. 2015. PMID: 26807165 Free PMC article. Review.
Cited by
-
Selective de-repression of germ cell-specific genes in mouse embryonic fibroblasts in a permissive epigenetic environment.Sci Rep. 2016 Sep 9;6:32932. doi: 10.1038/srep32932. Sci Rep. 2016. PMID: 27608931 Free PMC article.
-
G9a selectively represses a class of late-replicating genes at the nuclear periphery.Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19363-8. doi: 10.1073/pnas.0906142106. Epub 2009 Nov 4. Proc Natl Acad Sci U S A. 2009. PMID: 19889976 Free PMC article.
-
Cooperativity of co-factor NR2F2 with Pioneer Factors GATA3, FOXA1 in promoting ERα function.Theranostics. 2019 Aug 21;9(22):6501-6516. doi: 10.7150/thno.34874. eCollection 2019. Theranostics. 2019. PMID: 31588232 Free PMC article.
-
STREAMING-tag system reveals spatiotemporal relationships between transcriptional regulatory factors and transcriptional activity.Nat Commun. 2022 Dec 20;13(1):7672. doi: 10.1038/s41467-022-35286-2. Nat Commun. 2022. PMID: 36539402 Free PMC article.
-
Live imaging of transcription sites using an elongating RNA polymerase II-specific probe.J Cell Biol. 2022 Feb 7;221(2):e202104134. doi: 10.1083/jcb.202104134. Epub 2021 Dec 2. J Cell Biol. 2022. PMID: 34854870 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials