Phosphorylation of the carboxy-terminal domain of histone H1 : effects on secondary structure and DNA condensation
Roque Córdova, Alicia ![ORCID Identifier](/img/uab/orcid.ico)
(Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Ponte Marull, Immaculada, ![ORCID Identifier](/img/uab/orcid.ico)
dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Arrondo, José Luis R. (Universidad del País Vasco. Departamento de Bioquímica y Biología Molecular)
Suau, Pedro ![ORCID Identifier](/img/uab/orcid.ico)
(Universidad del País Vasco. Departamento de Bioquímica y Biología Molecular)
Date: |
2008 |
Abstract: |
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 α-helix. Partial phosphorylation increased the amount of undefined structure and decreased that of α-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. |
Grants: |
Ministerio de Educación, Cultura y Deporte BFU2005-02143
|
Rights: |
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Language: |
Anglès |
Document: |
Article ; recerca ; Versió publicada |
Published in: |
Nucleic acids research, Vol. 36 (7 2008) , p. 4719-4726, ISSN 1362-4962 |
DOI: 10.1093/nar/gkn440
PMID: 18632762
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Record created 2017-12-20, last modified 2022-10-05