4.8 Article

Structural Basis of Heterochromatin Formation by Human HP1

期刊

MOLECULAR CELL
卷 69, 期 3, 页码 385-+

出版社

CELL PRESS
DOI: 10.1016/j.molcel.2017.12.011

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资金

  1. JSPS KAKENHI [JP25116002, JP17H01408, JP16K18473]
  2. JST CREST [JPMJCR16G1]
  3. Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research [BINDS]) from the Japan Agency for Medical Research and Development (AMED)
  4. Waseda Research Institute for Science and Engineering
  5. Waseda University
  6. OIST
  7. Grants-in-Aid for Scientific Research [16K18473] Funding Source: KAKEN

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Heterochromatin plays important roles in transcriptional silencing and genome maintenance by the formation of condensed chromatin structures, which determine the epigenetic status of eukaryotic cells. The trimethylation of histone H3 lysine 9 (H3K9me3), a target of heterochromatin protein 1 (HP1), is a hallmark of heterochromatin formation. However, the mechanism by which HP1 folds chromatin-containing H3K9me3 into a higher-order structure has not been elucidated. Here we report the three-dimensional structure of the H3K9me3-containing dinucleosomes complexed with human HP1 alpha, HP1 beta, and HP1 gamma, determined by cryogenic electron microscopy with a Volta phase plate. In the structures, two H3K9me3 nucleosomes are bridged by a symmetric HP1 dimer. Surprisingly, the linker DNA between the nucleosomes does not directly interact with HP1, thus allowing nucleosome remodeling by the ATP-utilizing chromatin assembly and remodeling factor (ACF). The structure depicts the fundamental architecture of heterochromatin.

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