Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021 Apr:67:153-160.
doi: 10.1016/j.sbi.2020.10.018. Epub 2020 Dec 3.

Histone tails as signaling antennas of chromatin

Yunhui Peng  1 , Shuxiang Li  2 , David Landsman  1 , Anna R Panchenko  3
Affiliations
Review

Histone tails as signaling antennas of chromatin

Yunhui Peng et al. Curr Opin Struct Biol. 2021 Apr.

Abstract

Histone tails, representing the N-terminal or C-terminal regions flanking the histone core, play essential roles in chromatin signaling networks. Intrinsic disorder of histone tails and their propensity for post-translational modifications allow them to serve as hubs in coordination of epigenetic processes within the nucleosomal context. Deposition of histone variants with distinct histone tail properties further enriches histone tails' repertoire in epigenetic signaling. Given the advances in experimental techniques and in silico modelling, we review the most recent data on histone tails' effects on nucleosome stability and dynamics, their function in regulating chromatin accessibility and folding. Finally, we discuss different molecular mechanisms to understand how histone tails are involved in nucleosome recognition by binding partners and formation of higher-order chromatin structures.

PubMed Disclaimer

Figures

Figure 1.
Figure 1.
Intrinsically disordered histone tails perform their functions through different molecular mechanisms. (a) Fuzzy interactions of H1 tails stabilize the importin7-importinβ complex in histone transport (PDB: 6N88). H1 C-terminal domain can bind to acidic residues located near the importin7-importinβ binding interfaces through transient and non-specific electrostatic interactions. (b) Binding of H3 tails to ADD domain of DNMT3A allosterically induces the transition of DNMT3A from autoinhibitory state to the active state (PDB: 4UTP, 4U7T). Molecular surfaces are rendered in magenta (ADD domain of DNMT3A), cyan (catalytic domain of DNMT3A) and green (DNMT3L).
Figure 2.
Figure 2.
Mechanisms of regulation of nucleosome dynamics and interactions through histone tails. (a) Extensive and transient tail-DNA interactions in nucleosome and tail displacement mechanism of nucleosome recognition. (b) PTMs and mutations in histone tails modulate tail-DNA interactions and accessibility of DNA and tails in nucleosome. (c) Histone tail cleavage regulates nucleosome dynamics and interactions.
Figure 3.
Figure 3.
Representative binding modes between disordered histone tails and nucleosomal DNA observed in molecular dynamics simulations. The cartoon representations of histone core domains are hidden for clarifications.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ: Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997, 389:251–260. - PubMed

    1. Pilotto S, Speranzini V, Tortorici M, Durand D, Fish A, Valente S, Forneris F, Mai A, Sixma TK, Vachette P, et al.: Interplay among nucleosomal DNA, histone tails, and corepressor CoREST underlies LSD1-mediated H3 demethylation. Proc Natl Acad Sci U S A 2015, 112:2752–2757.

      *Authors propose a tail displacement model for LSD1-mediated H3 demethylation where the interaction between the SANT2 domain and nucleosomal DNA displaces the H3 tails from DNA and make them avaibable for capture by the LSD1 active site.

    1. Zhang R, Erler J, Langowski J: Histone Acetylation Regulates Chromatin Accessibility: Role of H4K16 in Inter-nucleosome Interaction. Biophys J 2017, 112:450–459. - PMC - PubMed

    1. Morrison EA, Bowerman S, Sylvers KL, Wereszczynski J, Musselman CA: The conformation of the histone H3 tail inhibits association of the BPTF PHD finger with the nucleosome. Elife 2018, 7.

      **A study demonstrates that H3 tails extensively interact with nucleosome DNA which inhibits the binding activity of PHD finger to histone tail. It further shows that histone modifications and mutations weaken the tail-DNA interactions and increase the accessibiliy of histone tail.

    1. Stutzer A, Liokatis S, Kiesel A, Schwarzer D, Sprangers R, Soding J, Selenko P, Fischle W: Modulations of DNA Contacts by Linker Histones and Post-translational Modifications Determine the Mobility and Modifiability of Nucleosomal H3 Tails. Mol Cell 2016, 61:247–259. - PubMed

Publication types

LinkOut - more resources

  NODES
Association 1
twitter 2