Cover Image

Role of histone tails in structural stability of the nucleosome

Histone tails play an important role in nucleosome structure and dynamics. Here we investigate the effect of truncation of histone tails H3, H4, H2A and H2B on nucleosome structure with 100 ns all-atom molecular dynamics simulations. Tail domains of H3 and H2B show propensity of -helics formation du...

Full description

Saved in:
Bibliographic Details
Main Authors: Biswas, Mithun (Author) , Voltz, Karine (Author) , Smith, Jeremy C. (Author) , Langowski, Jörg (Author)
Format: Article (Journal)
Language:English
Published: December 15, 2011
In: PLoS Computational Biology
Year: 2011, Volume: 7, Issue: 12, Pages: 1-12
ISSN:1553-7358
DOI:10.1371/journal.pcbi.1002279
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1371/journal.pcbi.1002279
Verlag, lizenzpflichtig, Volltext: https://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.1002279
Get full text
Author Notes:Mithun Biswas, Karine Voltz, Jeremy C. Smith, Jörg Langowski
Description
Summary:Histone tails play an important role in nucleosome structure and dynamics. Here we investigate the effect of truncation of histone tails H3, H4, H2A and H2B on nucleosome structure with 100 ns all-atom molecular dynamics simulations. Tail domains of H3 and H2B show propensity of -helics formation during the intact nucleosome simulation. On truncation of H4 or H2B tails no structural change occurs in histones. However, H3 or H2A tail truncation results in structural alterations in the histone core domain, and in both the cases the structural change occurs in the H2A3 domain. We also find that the contacts between the histone H2A C terminal docking domain and surrounding residues are destabilized upon H3 tail truncation. The relation between the present observations and corresponding experiments is discussed.
Item Description:Gesehen am 24.03.2022
Physical Description:Online Resource
ISSN:1553-7358
DOI:10.1371/journal.pcbi.1002279

Similar Items