iScience (Mar 2022)

Characteristic H3 N-tail dynamics in the nucleosome core particle, nucleosome, and chromatosome

  • Ayako Furukawa,
  • Masatoshi Wakamori,
  • Yasuhiro Arimura,
  • Hideaki Ohtomo,
  • Yasuo Tsunaka,
  • Hitoshi Kurumizaka,
  • Takashi Umehara,
  • Yoshifumi Nishimura

Journal volume & issue
Vol. 25, no. 3
p. 103937

Abstract

Read online

Summary: The nucleosome core particle (NCP) comprises a histone octamer, wrapped around by ∼146-bp DNA, while the nucleosome additionally contains linker DNA. We previously showed that, in the nucleosome, H4 N-tail acetylation enhances H3 N-tail acetylation by altering their mutual dynamics. Here, we have evaluated the roles of linker DNA and/or linker histone on H3 N-tail dynamics and acetylation by using the NCP and the chromatosome (i.e., linker histone H1.4-bound nucleosome). In contrast to the nucleosome, H3 N-tail acetylation and dynamics are greatly suppressed in the NCP regardless of H4 N-tail acetylation because the H3 N-tail is strongly bound between two DNA gyres. In the chromatosome, the asymmetric H3 N-tail adopts two conformations: one contacts two DNA gyres, as in the NCP; and one contacts linker DNA, as in the nucleosome. However, the rate of H3 N-tail acetylation is similar in the chromatosome and nucleosome. Thus, linker DNA and linker histone both regulate H3-tail dynamics and acetylation.

Keywords