Conformational Change of Nucleosome Arrays prior to Phase Separation.

Autor:	Zhang M; The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, USA.; Applied Science and Technology Graduate Group, University of California, Berkeley, USA.; California Institute for Quantitative Biosciences, University of California, Berkeley, USA., Celis CD; California Institute for Quantitative Biosciences, University of California, Berkeley, USA.; Howard Hughes Medical Institute, University of California, Berkeley, USA., Liu J; The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, USA., Bustamante C; Applied Science and Technology Graduate Group, University of California, Berkeley, USA.; California Institute for Quantitative Biosciences, University of California, Berkeley, USA.; Howard Hughes Medical Institute, University of California, Berkeley, USA.; Department of Chemistry, University of California, Berkeley, USA.; Department of Physics, University of California, Berkeley, USA.; Department of Molecular and Cell Biology, University of California, Berkeley, USA.; Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, USA.; Kavli Energy Nanoscience Institute, University of California, Berkeley, USA., Ren G; The Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, USA.
Jazyk:	angličtina
Zdroj:	Research square [Res Sq] 2023 Jan 19. Date of Electronic Publication: 2023 Jan 19.
DOI:	10.21203/rs.3.rs-2460504/v1
Abstrakt:	Chromatin phase transition serves as a regulatory mechanism for eukaryotic transcription. Understanding this process requires the characterization of the nucleosome array structure in response to external stimuli prior to phase separation. However, the intrinsic flexibility and heterogeneity hinders the arrays' structure determination. Here we exploit advances in cryogenic electron tomography (cryo-ET) to determine the three-dimensional (3D) structure of each individual particle of mono-, di-, tri-, and tetranucleosome arrays. Statistical analysis reveals the ionic strength changes the angle between the DNA linker and nucleosome core particle (NCP), which regulate the overall morphology of nucleosome arrays. The finding that one-third of the arrays in the presence of H1 contain an NCP invaded by foreign DNA suggests an alternative function of H1 in constructing nucleosomal networks. The new insights into the nucleosome conformational changes prior to the intermolecular interaction stage extends our understanding of chromatin phase separation regulation.
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu