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dc.contributor.authorRoque, Alicia
dc.contributor.authorPonte, Inma
dc.contributor.authorRodríguez Arrondo, José Luis
dc.contributor.authorSuau, Pedro
dc.date.accessioned2014-04-01T16:54:26Z
dc.date.available2014-04-01T16:54:26Z
dc.date.issued2008-08
dc.identifier.citationNucleic acids research 36(14) : 4719-4726 (2008)es
dc.identifier.issn0305-1048
dc.identifier.urihttp://hdl.handle.net/10810/11906
dc.description.abstractLinker 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 -structure and decreased that of -helix. Partial phosphorylation increased the amount of undefined structure and decreased that of -helix without a significant increase in -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.es
dc.language.isoenges
dc.publisherOxford University Presses
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.subjectlysine rich histonees
dc.subjectinfrared spectroscopyes
dc.subjectcellcyclees
dc.subjectchromatines
dc.subjectproteinses
dc.subjectbindinges
dc.subjectdephosphorylationes
dc.subjectpeptidees
dc.subjectsiteses
dc.titlePhosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensationes
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.holder2008 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.es
dc.relation.publisherversionhttp://nar.oxfordjournals.org/content/36/14/4719.fulles
dc.identifier.doi10.1093/nar/gkn440
dc.departamentoesBioquímica y biología moleculares_ES
dc.departamentoeuBiokimika eta biologia molekularraes_ES
dc.subject.categoriaGENETICS AND HEREDITY


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