Histone H3 Tail Modifications Alter Structure and Dynamics of the H1 C-Terminal Domain Within Nucleosomes

Subhra Kanti Das,Ashok Kumar,Fanfan Hao, Amber R. Cutter DiPiazza,He Fang,Tae-Hee Lee,Jeffrey J. Hayes

JOURNAL OF MOLECULAR BIOLOGY（2023）

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摘要

•How the linker histone H1 C-terminal tail (CTD) condenses chromatin remains unclear.•smFRET shows the H1 CTD undergoes a drastic condensation upon binding to nucleosomes.•H1 CTD adopts both a broad range of static and dynamic structures.•Both dynamics and condensation are affected by a mimic of histone H3 tail acetylation.•H1 CTD reorganizes linker DNA, suggests alternative mode of H3 PTM function.

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关键词

Linker Histone H1,nucleosomes,Intrinsically discorded protein,single-molecule FRET,histone acetylation

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