Premium
Chromatin dynamics of unfolding and refolding controlled by the nucleosome repeat length and the linker and core histones
Author(s) -
Kobori Toshiro,
Iwamoto Satoshi,
Takeyasu Kunio,
Ohtani Toshio
Publication year - 2007
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20671
Subject(s) - chromatin , linker dna , nucleosome , chemistry , linker , histone , biophysics , chromatosome , dna , saccharomyces cerevisiae , histone h1 , crystallography , microbiology and biotechnology , biochemistry , yeast , biology , computer science , operating system
Chromatin is composed of genomic DNA and histones, forming a hierarchical architecture in the nucleus. The chromatin hierarchy is common among eukaryotes despite different intrinsic properties of the genome. To investigate an effect of the differences in genome organization, chromatin unfolding processes were comparatively analyzed using Schizosaccaromyces pombe , Saccharomyces cerevisiae , and chicken erythrocyte. NaCl titration showed dynamic changes of the chromatin. 400–1000 m M NaCl facilitated beads with ∼115 nm in diameter in S. pombe chromatin. A similar transition was also observed in S. cerevisiae chromatin. This process did not involve core histone dissociation from the chromatin, and the persistence length after the transition was ∼26 nm for S. pombe and ∼28 nm for S. cerevisiae , indicating a salt‐induced unfolding to “beads‐on‐a‐string” fibers. Reduced salt concentration recovered the original structure, suggesting that electrostatic interaction would regulate this discrete folding‐unfolding process. On the other hand, the linker histone was extracted from chicken chromatin at 400 m M NaCl, and AFM observed the “beads‐on‐a‐string” fibers around a nucleus. Unlike yeast chromatin, therefore, this unfolding was irreversible because of linker histone dissociation. These results indicate that the chromatin unfolding and refolding depend on the presence and absence of the linker histone, and the length of the linker DNA. © 2007 Wiley Periodicals, Inc. Biopolymers 85:295–307, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com