Histone tails and the H3 alphaN helix regulate nucleosome mobility and stability.
Nucleosomes fulfill the apparently conflicting roles of compacting DNA within eukaryotic genomes while permitting access to regulatory factors. Central to this is their ability to stably associate with DNA while retaining the ability to undergo rearrangements that increase access to the underlying DNA. Here, we have studied different aspects of nucleosome dynamics including nucleosome sliding, histone dimer exchange, and DNA wrapping within nucleosomes. We find that alterations to histone proteins, especially the histone tails and vicinity of the histone H3 alphaN helix, can affect these processes differently, suggesting that they are mechanistically distinct. This raises the possibility that modifications to histone proteins may provide a means of fine-tuning specific aspects of the dynamic properties of nucleosomes to the context in which they are located.
Ferreira
Helder
H
Division of Gene Regulation and Expression, The Wellcome Trust Biocentre, Department of Biochemistry, University of Dundee, Dundee, United Kingdom.
Somers
Joanna
J
Webster
Ryan
R
Flaus
Andrew
A
Owen-Hughes
Tom
T
D000409:Alanine / Q000378:metabolism; D000818:Animals; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D019281:Dimerization; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D009707:Nucleosomes / Q000378:metabolism*; D017354:Point Mutation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D029867:Xenopus Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014982:Xenopus laevis
D006657:Histones; D009707:Nucleosomes; D011994:Recombinant Proteins; D029867:Xenopus Proteins; D004247:DNA; D000409:Alanine