Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

Histone H3

  • Yan-Ming Xu
  • Yue Yao
  • Andy T. Y. Lau
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101644

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 with linker histones (histone H1), the nucleosome arrays are further organized into solenoid conformation and looping domain structures that occur in both interphase and metaphase chromatin. During cell division, global histone protein production is temporally elevated to meet the cellular demands since histone proteins are needed to be deposited into the newly replicated DNA strands before chromatin condensation and chromatids segregation could happen, which subsequently divided the genetic materials into daughter cells.

In the past half century, histone proteins have long been regarded as the bulk materials...

This is a preview of subscription content, log in to check access.

References

  1. Bannister AJ, Kouzarides T. Reversing histone methylation. Nature. 2005;436:1103–6.PubMedCrossRefGoogle Scholar
  2. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  3. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  4. 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.PubMedCrossRefGoogle Scholar
  5. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  6. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  7. 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.PubMedCrossRefGoogle Scholar
  8. Holliday R. Epigenetics: a historical overview. Epigenetics. 2006;1:76–80.PubMedCrossRefGoogle Scholar
  9. 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.PubMedCrossRefGoogle Scholar
  10. Kallappagoudar S, Yadav RK, Lowe BR, Partridge JF. Histone H3 mutations--a special role for H3.3 in tumorigenesis? Chromosoma. 2015;124:177–89.PubMedPubMedCentralCrossRefGoogle Scholar
  11. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  12. Kouzarides T. Chromatin modifications and their function. Cell. 2007;128:693–705.CrossRefPubMedPubMedCentralGoogle Scholar
  13. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  14. 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.PubMedCrossRefGoogle Scholar
  15. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  16. Struhl K. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 1998;12:599–606.PubMedCrossRefGoogle Scholar
  17. 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.PubMedCrossRefGoogle Scholar
  18. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  19. 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.PubMedPubMedCentralCrossRefGoogle Scholar
  20. 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.PubMedCrossRefGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Laboratory of Cancer Biology and Epigenetics, Department of Cell Biology and GeneticsShantou University Medical CollegeShantouChina