4.5 Article

Chromatin structure meets cryo-EM: Dynamic building blocks of the functional architecture

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ELSEVIER
DOI: 10.1016/j.bbagrm.2022.194851

Keywords

Chromatin; Nucleosome; Histone; Cryo-electron microscopy; Single particle analysis; Cryo-electron tomography

Funding

  1. JSPS KAKENHI [JP22K06098, JP20H00449]
  2. Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)) from AMED [JP22ama121009]
  3. JST ERATO Grant [JPMJER1901]

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Chromatin is a dynamic molecular complex that packages DNA in the nucleus of eukaryotic cells. Recent studies using cryo-EM have revealed the structural details of different chromatin units and their functions in the cell.
Chromatin is a dynamic molecular complex composed of DNA and proteins that package the DNA in the nucleus of eukaryotic cells. The basic structural unit of chromatin is the nucleosome core particle, composed of similar to 150 base pairs of genomic DNA wrapped around a histone octamer containing two copies each of four histones, H2A, H2B, H3, and H4. Individual nucleosome core particles are connected by short linker DNAs, forming a nucleosome array known as a beads-on-a-string fiber. Higher-order structures of chromatin are closely linked to nuclear events such as replication, transcription, recombination, and repair. Recently, a variety of chromatin structures have been determined by single-particle cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET), and their structural details have provided clues about the chromatin architecture functions in the cell. In this review, we highlight recent cryo-EM structural studies of a fundamental chromatin unit to clarify the functions of chromatin.

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