Dynamics of the nucleosomal histone H3 N-terminal tail revealed by high precision single-molecule FRET.

ABSTRACT: Chromatin compaction and gene accessibility are orchestrated by assembly and disassembly of nucleosomes. Although the disassembly process was widely studied, little is known about the structure and dynamics of the disordered histone tails, which play a pivotal role for nucleosome integrity. This is a gap filling experimental FRET study from the perspective of the histone H3 N-terminal tail (H3NtT) of reconstituted mononucleosomes. By systematic variation of the labeling positions we monitored the motions of the H3NtT relative to the dyad axis and linker DNA. Single-molecule FRET unveiled that H3NtTs do not diffuse freely but follow the DNA motions with multiple interaction modes with certain permitted dynamic transitions in the μs to ms time range. We also demonstrate that the H3NtT can al

SUBMITTER: Lehmann K 

PROVIDER: S-EPMC7026643 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature