Mesoscale simulations of two nucleosome-repeat length oligonucleosomes

Tamar Schlick, Ognjen Perišić

Research output: Contribution to journalArticle

Abstract

The compaction of chromatin, accessed through coarse-grained modeling and simulation, reveals different folding patterns as a function of the nucleosome repeat length (NRL), the presence of the linker histone, and the ionic strength. Our results indicate that the linker histone has negligible influence on short NRL fibers, whereas for longer NRL fibers it works like, and in tandem with, concentrated positive counterions to condense the chromatin fiber. Longer NRL fibers also exhibit structural heterogeneity, with solenoid-like conformations viable in addition to irregular zigzags. These features of chromatin and associated internucleosomal patterns presented here help interpret structural dependencies of the chromatin fiber on internal and external factors. In particular, we suggest that longer-NRL are more advantageous for packing and achieving various levels of fiber compaction throughout the cell cycle.

Original languageEnglish (US)
Pages (from-to)10729-10737
Number of pages9
JournalPhysical Chemistry Chemical Physics
Volume11
Issue number45
DOIs
StatePublished - 2009

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Nucleosomes
chromatin
Chromatin
fibers
Fibers
simulation
Histones
Compaction
Solenoids
solenoids
Ionic strength
folding
Conformations
Cells
cycles

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Physics and Astronomy(all)

Cite this

Mesoscale simulations of two nucleosome-repeat length oligonucleosomes. / Schlick, Tamar; Perišić, Ognjen.

In: Physical Chemistry Chemical Physics, Vol. 11, No. 45, 2009, p. 10729-10737.

Research output: Contribution to journalArticle

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