Interaction of chromatin with a histone H1 containing swapped N- and C-terminal domains

Interaction of chromatin with a histone H1 containing swapped N- and C-terminal domains

Although the details of the structural involvement of histone H1 in the organization of the nucleosome are quite well understood, the sequential events involved in the recognition of its binding site are not as well known. We have used a recombinant human histone H1 (H1.1) in which the N- and C-term...

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Bibliographic Details
Published in:Bioscience reports Vol. 35; no. 3
Main Authors: Hutchinson, Jordana B, Cheema, Manjinder S, Wang, Jason, Missiaen, Krystal, Finn, Ron, Gonzalez Romero, Rodrigo, Th'ng, John P H, Hendzel, Michael, Ausió, Juan
Format: Journal Article
Language:English
Published: England Portland Press Ltd 01-06-2015
Subjects:
Binding Sites
Chromatin - metabolism
Chromatin - ultrastructure
Circular Dichroism
HeLa Cells
Histones - genetics
Histones - metabolism
Humans
Nucleosomes - metabolism
Original Paper
Original Papers
Protein Domains
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
analytical ultracentrifuge
FRAP
histones
circular dichroism
chromatin
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Summary:Although the details of the structural involvement of histone H1 in the organization of the nucleosome are quite well understood, the sequential events involved in the recognition of its binding site are not as well known. We have used a recombinant human histone H1 (H1.1) in which the N- and C-terminal domains (NTD/CTD) have been swapped and we have reconstituted it on to a 208-bp nucleosome. We have shown that the swapped version of the protein is still able to bind to nucleosomes through its structurally folded wing helix domain (WHD); however, analytical ultracentrifuge analysis demonstrates its ability to properly fold the chromatin fibre is impaired. Furthermore, FRAP analysis shows that the highly dynamic binding association of histone H1 with the chromatin fibre is altered, with a severely decreased half time of residence. All of this suggests that proper binding of histone H1 to chromatin is determined by the simultaneous and synergistic binding of its WHD-CTD to the nucleosome.
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Present address: Department of Medical Cell Biology, American University of Antigua College of Medicine, Coolidge, Antigua.
ISSN:0144-8463
1573-4935
DOI:10.1042/BSR20150087