Histone Acetylation and Disease

Annick Harel‐Bellan, Institut Andre Lwoff, Villejuif, France
Valentina Guasconi, Institut Andre Lwoff, Villejuif, France
Lauriane Fritsch, Institut Andre Lwoff, Villejuif, France
Redha Sekhri, Institut Andre Lwoff, Villejuif, France
Heike Lehrmann, Institut Andre Lwoff, Villejuif, France
Slimane Ait‐Si‐Ali, Institut Andre Lwoff, Villejuif, France

Published online: January 2006

DOI: 10.1038/npg.els.0006032

Acetylation of nucleosomal core histones plays a key regulatory role in many physiological processes such as proliferation and differentiation. Aberrant acetylation or deacetylation of histones leads to severe human diseases such as leukemia, epithelial cancers, fragile X-syndrome and Rubinstein–Taybi syndrome.

Keywords: histone acetyltransferase; histone deacetylase; histone, chromatin; leukemia

Figure 1. Mode of action of histone acetyltransferases (HAT) enzymes. At the level of gene promoter sequences, HAT can acetylate histones in nucleosomes (depicted by white cylinders), as well as nonhistone proteins such as proteins of the RNA polymerase complex (RNA pol II), sequence-specific transcription factors (TF) or cofactors. Arrows represent enzymatic activity. Ac: acetyl group; RNA: ribonucleic acid polymerase II; TF: transcription factors.
close
 References
    Ait-Si-Ali S, Polesskaya A, Filleur S, et al. (2000) CBP/p300 histone acetyl-transferase activity is important for the G1/S transition. Oncogene 19(20): 2430–2437.
    Jenuwein T and Allis CD (2001) Translating the histone code. Science 293(5532): 1074–1080.
    Magnaghi-Jaulin L, Ait-Si-Ali S and Harel-Bellan A (2000) Histone acetylation and the control of the cell cycle. Progress in Cell Cycle Research 4: 41–47.
    Marmorstein R and Roth SY (2001) Histone acetyltransferases: function, structure, and catalysis. Current Opinion in Genetics and Development 11(2): 155–61.
    Narlikar GJ, Fan HY and Kingston RE (2002) Cooperation between complexes that regulate chromatin structure and transcription. Cell 108(4): 475–487.
    Timmermann S, Lehrmann H, Polesskaya A, et al. (2001) Histone acetylation and disease. Cellular and Molecular Life Sciences: CMLS 58(5,6): 728–736.
    Torchia J, Glass C and Rosenfeld MG (1998) Co-activators and co-repressors in the integration of transcriptional responses. Current Opinion in Cellular Biology 10(3): 373–383.
 Web Links
    ePath CREBBP, (CREB binding protein (Rubinstein–Taybi syndrome)); Locus ID: 1387. LocusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?l=1387
    ePath FMR1 (fragile X mental retardation 1); Locus ID: 2332. LocusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?l=2332
    ePath MECP2 (methyl CpG binding protein 2 (Rett syndrome)); Locus ID: 4204. LocusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?l=4204
    ePath SMARCA4 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4); Locus ID: 6597. LocusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?l=6597
    ePath TP53 (tumor protein p53 (Li–Fraumeni syndrome)); Locus ID: 7157. LocusLink: http://www.ncbi.nlm.nih.gov/LocusLink/LocRpt.cgi?l=7157
    ePath CREBBP (CREB binding protein (Rubinstein–Taybi syndrome)); MIM number: 600140. OMIM: http://www.ncbi.nlm.nih.gov/htbin-post/Omim/dispmim?600140
    ePath FMR1 (fragile X mental retardation 1); MIM number: 309550. OMIM: http://www.ncbi.nlm.nih.gov/htbin-post/Omim/dispmim?309550
    ePath MECP2 (methyl CpG binding protein 2 (Rett syndrome)); MIM number: 300005. OMIM: http://www.ncbi.nlm.nih.gov/htbin-post/Omim/dispmim?300005
    ePath SMARCA4 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4); MIM number: 603254. OMIM: http://www.ncbi.nlm.nih.gov/htbin-post/Omim/dispmim?603254
    ePath TP53 (tumor protein p53 (Li–Fraumeni syndrome)); MIM number: 191170. OMIM: http://www.ncbi.nlm.nih.gov/htbin-post/Omim/dispmim?191170

Related Sub-Topics:

Cell Biology of Cancer | Cell Cycle | Growth and Synthesis | Molecular Genetics of Common and Complex Disease | Cancer Genetics | Gene and Genome Structure and Organisation | Epigenetics and Disease | Transcriptional Regulation | Chromosomes and Chromatin Modifications
Contact Editor close
Submit a note to the editor about this article by filling in the form below.

* Required Field

Article Title: Histone Acetylation and Disease
 
How to Cite close
Harel‐Bellan, Annick, Guasconi, Valentina, Fritsch, Lauriane, Sekhri, Redha, Lehrmann, Heike, and Ait‐Si‐Ali, Slimane(Jan 2006) Histone Acetylation and Disease. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0006032]