Synonyms
H3 histone family, member A; H3/A; H31; H3FA; H3FB; H3FC; H3FD; H3FF; H3FH; H3FI; H3FJ; H3FK; H3FL; HIST1H3A; HIST1H3B; HIST1H3C; HIST1H3D; HIST1H3E; HIST1H3F; HIST1H3G; HIST1H3H; HIST1H3I; HIST1H3J; histone 1, H3a; histone cluster 1, H3a; Histone H3.1; Histone H3/a; Histone H3/b; Histone H3/c; Histone H3/d; Histone H3/f; Histone H3/h; Histone H3/i; Histone H3/j; Histone H3/k; Histone H3/l
H3 histone family, member M; H3 histone, family 2; histone 2, H3c; histone H3.2; histone H3/m; histone H3/o
H3 histone, family 3A; H3 histone, family 3B (H3.3B); H3.3A; H3.3B; H33; H3F3; H3F3A; H3F3B; Histone H3.3
Historical Background
The eukaryotic genome is extraordinarily well organized. This is achieved through the winding of DNA to form continuous arrays of nucleosome, the fundamental repeating unit of chromatin. Each nucleosome consists of ~147 base pairs of DNA wrapped around a core histone octamer (two copies each of histone H2A, H2B, H3, and H4). Based on this, by the association...
This is a preview of subscription content, log in via an institution.
References
Bannister AJ, Kouzarides T. Reversing histone methylation. Nature. 2005;436:1103–6.
Britton LM, Newhart A, Bhanu NV, Sridharan R, Gonzales-Cope M, Plath K, et al. Initial characterization of histone H3 serine 10 O-acetylation. Epigenetics. 2013;8:1101–13.
Chen Y, Sprung R, Tang Y, Ball H, Sangras B, Kim SC, et al. Lysine propionylation and butyrylation are novel post-translational modifications in histones. Mol Cell Proteomics. 2007;6:812–9.
Dai L, Peng C, Montellier E, Lu Z, Chen Y, Ishii H, et al. Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark. Nat Chem Biol. 2014;10:365–70.
Fong JJ, Nguyen BL, Bridger R, Medrano EE, Wells L, Pan S, Sifers RN. β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3. J Biol Chem. 2012;287:12195–203.
García-Giménez JL, Òlaso G, Hake SB, Bönisch C, Wiedemann SM, Markovic J, et al. Histone H3. glutathionylation in proliferating mammalian cells destabilizes nucleosomal structure. Antioxid Redox Signal. 2013;19:1305–20.
Hinchcliffe EH, Day CA, Karanjeet KB, Fadness S, Langfald A, Vaughan KT, Dong Z. Chromosome missegregation during anaphase triggers p53 cell cycle arrest through histone H3.3 Ser31 phosphorylation. Nat Cell Biol. 2016;18:668–75.
Holliday R. Epigenetics: a historical overview. Epigenetics. 2006;1:76–80.
Jiang T, Zhou X, Taghizadeh K, Dong M, Dedon PC. N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage. Proc Natl Acad Sci USA. 2007;104:60–5.
Kallappagoudar S, Yadav RK, Lowe BR, Partridge JF. Histone H3 mutations--a special role for H3.3 in tumorigenesis? Chromosoma. 2015;124:177–89.
Kothapalli N, Camporeale G, Kueh A, Chew YC, Oommen AM, Griffin JB, Zempleni J. Biological functions of biotinylated histones. J Nutr Biochem. 2005;16:446–8.
Kouzarides T. Chromatin modifications and their function. Cell. 2007;128:693–705.
Maze I, Noh KM, Soshnev AA, Allis CD. Every amino acid matters: essential contributions of histone variants to mammalian development and disease. Nat Rev Genet. 2014;15:259–71.
Monks TJ, Xie R, Tikoo K, Lau SS. Ros-induced histone modifications and their role in cell survival and cell death. Drug Metab Rev. 2006;38:755–67.
Sabari BR, Tang Z, Huang H, Yong-Gonzalez V, Molina H, Kong HE, et al. Intracellular crotonyl-CoA stimulates transcription through p300-catalyzed histone crotonylation. Mol Cell. 2015;58:203–15.
Struhl K. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 1998;12:599–606.
Wang H, Zhai L, Xu J, Joo HY, Jackson S, Erdjument-Bromage H, et al. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol Cell. 2006;22:383–94.
Xie Z, Dai J, Dai L, Tan M, Cheng Z, Wu Y, et al. Lysine succinylation and lysine malonylation in histones. Mol Cell Proteomics. 2012;11:100–7.
Xie Z, Zhang D, Chung D, Tang Z, Huang H, Dai L, et al. Metabolic regulation of gene expression by histone lysine β-hydroxybutyrylation. Mol Cell. 2016;62:194–206.
Zhang Y, Reinberg D. Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev. 2001;15:2343–60.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2016 Springer Science+Business Media LLC
About this entry
Cite this entry
Xu, YM., Yao, Y., Lau, A.T.Y. (2016). Histone H3. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_101644-1
Download citation
DOI: https://doi.org/10.1007/978-1-4614-6438-9_101644-1
Received:
Accepted:
Published:
Publisher Name: Springer, New York, NY
Online ISBN: 978-1-4614-6438-9
eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences