Nano-scale analyses of the chromatin decompaction induced by histone acetylation

DOI Web Site 被引用文献3件 参考文献86件
  • Hizume Kohji
    Laboratory of Plasma Membrane and Nuclear Signaling, Graduate School of Biostudies, Kyoto University Division of Microbial Genetics, National Institute of Genetics, Research Organization of Information and Systems
  • Araki Sumiko
    Department of Physics, Graduate School of Science, Kyoto University
  • Hata Kosuke
    Laboratory of Plasma Membrane and Nuclear Signaling, Graduate School of Biostudies, Kyoto University
  • Prieto Eloise
    Laboratory of Plasma Membrane and Nuclear Signaling, Graduate School of Biostudies, Kyoto University
  • Kundu Tapas K.
    Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Center for Advanced Scientific Research
  • Yoshikawa Kenichi
    Department of Physics, Graduate School of Science, Kyoto University
  • Takeyasu Kunio
    Laboratory of Plasma Membrane and Nuclear Signaling, Graduate School of Biostudies, Kyoto University

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The acetylation of histone tails is a key factor in the maintenance of chromatin dynamics and cellular homeostasis. The hallmark of active chromatin is the hyper-acetylation of histones, which appears to result in a more open chromatin structure. Although short nucleosomal arrays have been studied, the structural dynamics of relatively long acetylated chromatin remain unclear. We have analyzed in detail the structure of long hyper-acetylated chromatin fibers using atomic force microscopy (AFM). Hyper-acetylated chromatin fibers isolated from nuclei that had been treated with Trichostatin A (TSA), an inhibitor of histone deacetylase, were found to be thinner than those from untreated nuclei. The acetylated chromatin fibers were more easily spread out of nuclei by high-salt treatment, implying that hyper-acetylation facilitates the release of chromatin fibers from compact heterochromatin regions. Chromatin fibers reconstituted in vitro from core histones and linker histone H1 became thinner upon acetylation. AFM imaging indicated that the gyration radius of the nucleosomal fiber increased after acetylation and that the hyper-acetylated nucleosomes did not aggregate at high salt concentrations, in contrast to the behavior of non-acetylated nucleosomal arrays, suggesting that acetylation increases long-range repulsions between nucleosomes. Based on these data, we considered a simple coarse grained model, which underlines the effect of remaining electric charges inside the chromatin fiber.

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