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Direct Observation of H3–H4 Octasome by High‐Speed AFM
Author(s) -
Zou Tingting,
Hashiya Fumitaka,
Wei Yulei,
Yu Zutao,
Pandian Ganesh N.,
Sugiyama Hiroshi
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201804010
Subject(s) - nucleosome , histone , histone octamer , micrococcal nuclease , histone code , histone h1 , histone methylation , chemistry , histone h2a , biophysics , chromatosome , histone h3 , atomic force microscopy , dna , microbiology and biotechnology , biochemistry , biology , materials science , nanotechnology , dna methylation , gene expression , gene
Despite evidence that histone H3 and H4 proteins may act as the precursor for orientating the DNA sequence to form nucleosome structures, there is no direct evidence of the formed compact structure. Here, it is demonstrated that a histone H3–H4 octasome could be constructed without the involvement of histone H2A–H2B under in vitro reconstitution conditions. Atomic force microscopy was used to obtain the first direct observation of the octasome structure, which exhibited a similar core‐protein size as that of a nucleosome but with a shorter core histone‐binding DNA region. The octasome also displayed a one‐step histone‐dissociation pattern under heat treatment, distinct micrococcal nuclease and peplomycin accessibility, which suggests a different wrapping pattern to that in nucleosomes.