» Articles » PMID: 26474904

The Interplay of Histone Modifications - Writers That Read

Overview
Journal EMBO Rep
Specialty Molecular Biology
Date 2015 Oct 18
PMID 26474904
Citations 372
Authors
Affiliations
Soon will be listed here.
Abstract

Histones are subject to a vast array of posttranslational modifications including acetylation, methylation, phosphorylation, and ubiquitylation. The writers of these modifications play important roles in normal development and their mutation or misregulation is linked with both genetic disorders and various cancers. Readers of these marks contain protein domains that allow their recruitment to chromatin. Interestingly, writers often contain domains which can read chromatin marks, allowing the reinforcement of modifications through a positive feedback loop or inhibition of their activity by other modifications. We discuss how such positive reinforcement can result in chromatin states that are robust and can be epigenetically maintained through cell division. We describe the implications of these regulatory systems in relation to modifications including H3K4me3, H3K79me3, and H3K36me3 that are associated with active genes and H3K27me3 and H3K9me3 that have been linked to transcriptional repression. We also review the crosstalk between active and repressive modifications, illustrated by the interplay between the Polycomb and Trithorax histone-modifying proteins, and discuss how this may be important in defining gene expression states during development.

Citing Articles

Histone H3 lysine 9 tri-methylation is associated with pterygium.

Choi D, Na A, Jeoung S, Choi Y, Park N, Park H BMC Ophthalmol. 2025; 25(1):106.

PMID: 40033254 PMC: 11874390. DOI: 10.1186/s12886-025-03939-7.


Regulation of chromatin modifications through coordination of nucleus size and epithelial cell morphology heterogeneity.

Bermudez A, Latham Z, Ma A, Bi D, Hu J, Lin N Commun Biol. 2025; 8(1):269.

PMID: 39979587 PMC: 11842846. DOI: 10.1038/s42003-025-07677-w.


Epigenetic memory as crucial contributing factor in directing the differentiation of human iPSC into pancreatic β-cells in vitro.

Diane A, Mu-U-Min R, Al-Siddiqi H Cell Tissue Res. 2025; 399(3):267-276.

PMID: 39883142 PMC: 11870940. DOI: 10.1007/s00441-025-03952-8.


Prediction of gene expression using histone modification patterns extracted by Particle Swarm Optimization.

Paul N, Wolber J, Sahrhage M, Beissbarth T, Haubrock M Bioinformatics. 2025; 41(2).

PMID: 39878927 PMC: 11802466. DOI: 10.1093/bioinformatics/btaf033.


The role of lncRNAs in the interplay of signaling pathways and epigenetic mechanisms in glioma.

Bora Yildiz C, Du J, Mohan K, Zimmer-Bensch G, Abdolahi S Epigenomics. 2025; 17(2):125-140.

PMID: 39829063 PMC: 11792803. DOI: 10.1080/17501911.2024.2442297.


References
1.
Wu L, Lee S, Zhou B, Nguyen U, Muir T, Tan S . ASH2L regulates ubiquitylation signaling to MLL: trans-regulation of H3 K4 methylation in higher eukaryotes. Mol Cell. 2013; 49(6):1108-20. PMC: 3615107. DOI: 10.1016/j.molcel.2013.01.033. View

2.
Brien G, Gambero G, OConnell D, Jerman E, Turner S, Egan C . Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to embryonic stem cell genes during differentiation. Nat Struct Mol Biol. 2012; 19(12):1273-81. DOI: 10.1038/nsmb.2449. View

3.
Peters A, Kubicek S, Mechtler K, OSullivan R, Derijck A, Perez-Burgos L . Partitioning and plasticity of repressive histone methylation states in mammalian chromatin. Mol Cell. 2003; 12(6):1577-89. DOI: 10.1016/s1097-2765(03)00477-5. View

4.
Yuan W, Xu M, Huang C, Liu N, Chen S, Zhu B . H3K36 methylation antagonizes PRC2-mediated H3K27 methylation. J Biol Chem. 2011; 286(10):7983-7989. PMC: 3048685. DOI: 10.1074/jbc.M110.194027. View

5.
Ng H, Ciccone D, Morshead K, Oettinger M, Struhl K . Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: a potential mechanism for position-effect variegation. Proc Natl Acad Sci U S A. 2003; 100(4):1820-5. PMC: 149917. DOI: 10.1073/pnas.0437846100. View