第21回日本蛋白質科学会年会

講演情報

ポスターセッション

[1P-2] ポスター1(1P-49ー1P-87)

2021年6月16日(水) 14:45 〜 16:45 ポスター会場2

[1P-50*] 高速AFMによるヒストンH2AトポグラフィーとそのDNAコンパクション時の時空間ダイナミクスの解明

西出 梧朗1, Keesiang Lim2,3, 小林 亜紀子2,3, 羽澤 勝治2,3, 中山 隆宏2, 古寺 哲幸2, 安藤 敏夫2, Wong Richard2,3 (1.金大・新学術・ナノ, 2.金大・新学術・WPI-NanoLSI, 3.金大・新学術・セルバイオ)

DNA wrapping on histone octamers is crucial for DNA compaction to store enormous biological data in nuclei. Two copies each of histones H2A, H2B, H3 and H4 are collected by histone chaperones and chromatin remodelers. Each nucleosome is built up of 50 nm of DNA (147 bp) that is wrapped 1.7 times around a histone octamer. Nucleosomes are dynamic as they can either relocate or spontaneously breathe. DNA-histone interaction is mainly mediated by electrostatic force, and manipulation of this force is essential for regulating biological activities such as DNA repair and gene expression. Much less is known about the dynamics of interaction between a single histone and DNA, due to lack of suitable nanoscopic imaging tools. Here we investigate the topology properties of H2A and its interaction with plasmid DNA in physiological buffer using high-speed atomic force microscopy (HS-AFM). HS-AFM images show that H2A topology resembles to its simulated images, in which H2A tail can be clearly seen. Ongoing works regarding HS-AFM imaging of interaction between H2A and plasmid DNA will be discussed during poster presentation.