Publikation:

HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding

Vorschaubild

Dateien

Zu diesem Dokument gibt es keine Dateien.

Datum

2005

Autor:innen

Daujat, Sylvain
Zeissler, Ulrike
Happel, Nicole
Schneider, Robert

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

URI (zitierfähiger Link)
DOI (zitierfähiger Link)
https://doi.org/10.1074/jbc.C500229200
ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung

Sammlungen

Biologie: Publikationen
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

The Journal of Biological Chemistry. 2005, 280(45), pp. 38090-38095. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.C500229200

Zusammenfassung

Histone lysine methylation can have positive or negative effects on transcription, depending on the precise methylation site. According to the "histone code" hypothesis these methylation marks can be read by proteins that bind them specifically and then regulate downstream events. Hetero-chromatin protein 1 (HP1), an essential component of heterochromatin, binds specifically to methylated Lys9 of histone H3 (K9/H3). The linker histone H1.4 is methylated on Lys26 (K26/H1.4), but the role of this methylation in downstream events remains unknown. Here we identify HP1 as a protein specifically recognizing and binding to methylated K26/H1.4. We demonstrate that the Chromo domain of HP1 is mediating this binding and that phosphorylation of Ser27 on H1.4 (S27/H1.4) prevents HP1 from binding. We suggest that methylation of K26/H1.4 could have a role in tethering HP1 to chromatin and that this could also explain how HP1 is targeted to those regions of chromatin where it does not colocalize with methylated K9/H3. Our results provide the first experimental evidence for a "phospho switch" model in which neighboring phosphorylation reverts the effect of histone lysine methylation.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690DAUJAT, Sylvain, Ulrike ZEISSLER, Tanja WALDMANN, Nicole HAPPEL, Robert SCHNEIDER, 2005. HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding. In: The Journal of Biological Chemistry. 2005, 280(45), pp. 38090-38095. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.C500229200
BibTex
@article{Daujat2005-11-11binds-38819,
  year={2005},
  doi={10.1074/jbc.C500229200},
  title={HP1 binds specifically to Lys<sup>26</sup>-methylated histone H1.4, whereas simultaneous Ser<sup>27</sup> phosphorylation blocks HP1 binding},
  number={45},
  volume={280},
  issn={0021-9258},
  journal={The Journal of Biological Chemistry},
  pages={38090--38095},
  author={Daujat, Sylvain and Zeissler, Ulrike and Waldmann, Tanja and Happel, Nicole and Schneider, Robert}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/38819">
    <dc:contributor>Happel, Nicole</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-09T12:29:42Z</dc:date>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Zeissler, Ulrike</dc:contributor>
    <dc:contributor>Schneider, Robert</dc:contributor>
    <dcterms:title>HP1 binds specifically to Lys&lt;sup&gt;26&lt;/sup&gt;-methylated histone H1.4, whereas simultaneous Ser&lt;sup&gt;27&lt;/sup&gt; phosphorylation blocks HP1 binding</dcterms:title>
    <dc:creator>Happel, Nicole</dc:creator>
    <dc:contributor>Daujat, Sylvain</dc:contributor>
    <dc:creator>Waldmann, Tanja</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-09T12:29:42Z</dcterms:available>
    <dc:creator>Zeissler, Ulrike</dc:creator>
    <dc:language>eng</dc:language>
    <dcterms:issued>2005-11-11</dcterms:issued>
    <dc:creator>Schneider, Robert</dc:creator>
    <dc:contributor>Waldmann, Tanja</dc:contributor>
    <dcterms:abstract xml:lang="eng">Histone lysine methylation can have positive or negative effects on transcription, depending on the precise methylation site. According to the "histone code" hypothesis these methylation marks can be read by proteins that bind them specifically and then regulate downstream events. Hetero-chromatin protein 1 (HP1), an essential component of heterochromatin, binds specifically to methylated Lys&lt;sup&gt;9&lt;/sup&gt; of histone H3 (K9/H3). The linker histone H1.4 is methylated on Lys&lt;sup&gt;26&lt;/sup&gt; (K26/H1.4), but the role of this methylation in downstream events remains unknown. Here we identify HP1 as a protein specifically recognizing and binding to methylated K26/H1.4. We demonstrate that the Chromo domain of HP1 is mediating this binding and that phosphorylation of Ser&lt;sup&gt;27&lt;/sup&gt; on H1.4 (S27/H1.4) prevents HP1 from binding. We suggest that methylation of K26/H1.4 could have a role in tethering HP1 to chromatin and that this could also explain how HP1 is targeted to those regions of chromatin where it does not colocalize with methylated K9/H3. Our results provide the first experimental evidence for a "phospho switch" model in which neighboring phosphorylation reverts the effect of histone lysine methylation.</dcterms:abstract>
    <dc:creator>Daujat, Sylvain</dc:creator>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38819"/>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
Begutachtet
Diese Publikation teilen