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Nucleic Acids Research Advance Access published online on July 16, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn440
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Gene regulation, Chromatin and Epigenetics

Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation

Alicia Roque1, Inma Ponte1, José Luis R. Arrondo2 and Pedro Suau1,*

1Departamento de Bioquímica y Biología Molecular, Facultad de Biociencias, Universidad Autónoma de Barcelona, 08193 Bellaterra, Barcelona, Spain and 2Departamento de Bioquímica, Universidad del País Vasco, Apartado 644, E-48080, Bilbao, Spain

*To whom correspondence should be addressed. Tel: +34 93 5811391; Fax: +34 93 5811264; Email: pere.suau{at}uab.es

Received May 15, 2008. Revised June 26, 2008. Accepted June 26, 2008.

Linker histone H1 plays an important role in chromatin folding. Phosphorylation by cyclin-dependent kinases is the main post-translational modification of histone H1. We studied the effects of phosphorylation on the secondary structure of the DNA-bound H1 carboxy-terminal domain (CTD), which contains most of the phosphorylation sites of the molecule. The effects of phosphorylation on the secondary structure of the DNA-bound CTD were site-specific and depended on the number of phosphate groups. Full phosphorylation significantly increased the proportion of β-structure and decreased that of {alpha}-helix. Partial phosphorylation increased the amount of undefined structure and decreased that of {alpha}-helix without a significant increase in β-structure. Phosphorylation had a moderate effect on the affinity of the CTD for the DNA, which was proportional to the number of phosphate groups. Partial phosphorylation drastically reduced the aggregation of DNA fragments by the CTD, but full phosphorylation restored to a large extent the aggregation capacity of the unphosphorylated domain. These results support the involvement of H1 hyperphosphorylation in metaphase chromatin condensation and of H1 partial phosphorylation in interphase chromatin relaxation. More generally, our results suggest that the effects of phosphorylation are mediated by specific structural changes and are not simply a consequence of the net charge.


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