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Direct Observation of H3–H4 Octasome by High‐Speed AFM

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 o...

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Bibliographic Details
Published in:Chemistry : a European journal 2018-10, Vol.24 (60), p.15998-16002
Main Authors: Zou, Tingting, Hashiya, Fumitaka, Wei, Yulei, Yu, Zutao, Pandian, Ganesh N., Sugiyama, Hiroshi
Format: Article
Language:English
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Summary: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. It′s a wrap! Here it is demonstrated that a histone H3–H4 octasome can be constructed without involving histone H2A–H2B under in vitro reconstitution conditions. The first direct observation of the octasome structure was achieved by high speed atomic force microscopy, and it was found to exhibit a similar core‐protein size to a nucleosome but with a shorter core histone‐binding DNA region.
ISSN:0947-6539
1521-3765
DOI:10.1002/chem.201804010