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

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 contain...

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Detalhes bibliográficos
Autores: Roque, Alicia, Ponte, Inma, Rodríguez Arrondo, José Luis, Suau, Pedro
Formato: artículo
Fecha de publicación:2008
País:España
Recursos:Universidad del País Vasco
Repositorio:Addi. Archivo Digital para la Docencia y la Investigación
OAI Identifier:oai:addi.ehu.eus:10810/11906
Acesso em linha:http://hdl.handle.net/10810/11906
Access Level:acceso abierto
Palavra-chave:lysine rich histone
infrared spectroscopy
cellcycle
chromatin
proteins
binding
dephosphorylation
peptide
sites
GENETICS AND HEREDITY
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spelling Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensationRoque, AliciaPonte, InmaRodríguez Arrondo, José LuisSuau, Pedrolysine rich histoneinfrared spectroscopycellcyclechromatinproteinsbindingdephosphorylationpeptidesitesGENETICS AND HEREDITYLinker 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.Oxford University Press201420142008info:eu-repo/semantics/articleapplication/pdfapplication/pdfhttp://hdl.handle.net/10810/11906reponame:Addi. Archivo Digital para la Docencia y la Investigacióninstname:Universidad del País VascoIngléshttp://nar.oxfordjournals.org/content/36/14/4719.fullinfo:eu-repo/semantics/openAccess2008 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.oai:addi.ehu.eus:10810/119062026-06-18T09:23:17Z
dc.title.none.fl_str_mv Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
title Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
spellingShingle Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
Roque, Alicia
lysine rich histone
infrared spectroscopy
cellcycle
chromatin
proteins
binding
dephosphorylation
peptide
sites
GENETICS AND HEREDITY
title_short Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
title_full Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
title_fullStr Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
title_full_unstemmed Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
title_sort Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
dc.creator.none.fl_str_mv Roque, Alicia
Ponte, Inma
Rodríguez Arrondo, José Luis
Suau, Pedro
author Roque, Alicia
author_facet Roque, Alicia
Ponte, Inma
Rodríguez Arrondo, José Luis
Suau, Pedro
author_role author
author2 Ponte, Inma
Rodríguez Arrondo, José Luis
Suau, Pedro
author2_role author
author
author
dc.subject.none.fl_str_mv lysine rich histone
infrared spectroscopy
cellcycle
chromatin
proteins
binding
dephosphorylation
peptide
sites
GENETICS AND HEREDITY
topic lysine rich histone
infrared spectroscopy
cellcycle
chromatin
proteins
binding
dephosphorylation
peptide
sites
GENETICS AND HEREDITY
description 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 -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.
publishDate 2008
dc.date.none.fl_str_mv 2008
2014
2014
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10810/11906
url http://hdl.handle.net/10810/11906
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://nar.oxfordjournals.org/content/36/14/4719.full
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:Addi. Archivo Digital para la Docencia y la Investigación
instname:Universidad del País Vasco
instname_str Universidad del País Vasco
reponame_str Addi. Archivo Digital para la Docencia y la Investigación
collection Addi. Archivo Digital para la Docencia y la Investigación
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.228081

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