» Articles » PMID: 25306110

MacroH2A1.1 and PARP-1 Cooperate to Regulate Transcription by Promoting CBP-mediated H2B Acetylation

Overview
Date 2014 Oct 13
PMID 25306110
Citations 72
Authors
Affiliations
Soon will be listed here.
Abstract

The histone variant macroH2A1 regulates gene expression important for differentiation, stem-cell reprogramming and tumor suppression. Here, we demonstrate that in primary human cells, macroH2A1 participates in two physically and functionally distinct types of chromatin marked by either H3K27me3 or nine histone acetylations. Using RNA sequencing, we found that macroH2A1-regulated genes, which have roles in cancer progression, are specifically found in macroH2A1-containing acetylated chromatin. Of the two macroH2A1 variants, macroH2A1.1 and macroH2A1.2, the former is suppressed in cancer and can interact with PARP-generated poly(ADP-ribose). Through the recruitment of PARP-1, macroH2A1.1 promotes the CBP-mediated acetylation of H2B K12 and K120, which either positively or negatively regulates the expression of macroH2A1-target genes. Although macroH2A1-regulated H2B acetylation is a common feature of primary cells, this regulation is typically lost in cancer cells. Consequently, our results provide insight into macroH2A1.1's role in cancer suppression.

Citing Articles

Pan-cancer analysis of the transcriptional expression of histone acetylation enzymes in solid tumors defines a new classification scheme for gliomas.

Zhang J, Li L, Tang A, Wang C, Wang Y, Hu Y Front Immunol. 2025; 15:1523034.

PMID: 39906742 PMC: 11790639. DOI: 10.3389/fimmu.2024.1523034.


Transcriptome and acetylome profiling identify crucial steps of neuronal differentiation in Rubinstein-Taybi syndrome.

Van Gils J, Karkar S, Barre A, Ley-Ngardigal S, Nothof S, Claverol S Commun Biol. 2024; 7(1):1331.

PMID: 39407026 PMC: 11480426. DOI: 10.1038/s42003-024-06939-3.


The Function of H2A Histone Variants and Their Roles in Diseases.

Yin X, Zeng D, Liao Y, Tang C, Li Y Biomolecules. 2024; 14(8).

PMID: 39199381 PMC: 11352661. DOI: 10.3390/biom14080993.


Multifunctional histone variants in genome function.

Wong L, Tremethick D Nat Rev Genet. 2024; 26(2):82-104.

PMID: 39138293 DOI: 10.1038/s41576-024-00759-1.


Transcriptional regulation mechanism of PARP1 and its application in disease treatment.

Lu Y, Fu W, Xing W, Wu H, Zhang C, Xu D Epigenetics Chromatin. 2024; 17(1):26.

PMID: 39118189 PMC: 11308664. DOI: 10.1186/s13072-024-00550-w.


References
1.
Schiltz R, Mizzen C, Vassilev A, Cook R, Allis C, Nakatani Y . Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates. J Biol Chem. 1999; 274(3):1189-92. DOI: 10.1074/jbc.274.3.1189. View

2.
Rappa F, Greco A, Podrini C, Cappello F, Foti M, Bourgoin L . Immunopositivity for histone macroH2A1 isoforms marks steatosis-associated hepatocellular carcinoma. PLoS One. 2013; 8(1):e54458. PMC: 3553099. DOI: 10.1371/journal.pone.0054458. View

3.
Kraus W, Hottiger M . PARP-1 and gene regulation: progress and puzzles. Mol Aspects Med. 2013; 34(6):1109-23. DOI: 10.1016/j.mam.2013.01.005. View

4.
Hassa P, Buerki C, Lombardi C, Imhof R, Hottiger M . Transcriptional coactivation of nuclear factor-kappaB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1. J Biol Chem. 2003; 278(46):45145-53. DOI: 10.1074/jbc.M307957200. View

5.
Schefe J, Lehmann K, Buschmann I, Unger T, Funke-Kaiser H . Quantitative real-time RT-PCR data analysis: current concepts and the novel "gene expression's CT difference" formula. J Mol Med (Berl). 2006; 84(11):901-10. DOI: 10.1007/s00109-006-0097-6. View