WeightNameValue
1000 Titel
  • Methylation of Lysine 9 in Histone H3 Directs Alternative Modes of Highly Dynamic Interaction of Heterochromatin Protein hHP1β with the Nucleosome
1000 Autor/in
  1. Munari, Francesca |
  2. Soeroes, Szabolcs |
  3. Zenn, Hans Michael |
  4. Schomburg, Adrian |
  5. Kost, Nils |
  6. Schröder, Sabrina |
  7. Klingberg, Rebecca |
  8. Rezaei-Ghaleh, Nasrollah |
  9. Stützer, Alexandra |
  10. Gelato, Kathy Ann |
  11. Walla, Peter Jomo |
  12. Becker, Stefan |
  13. Schwarzer, Dirk |
  14. Zimmermann, Bastian |
  15. Fischle, Wolfgang |
  16. Zweckstetter, Markus |
1000 Erscheinungsjahr 2012
1000 LeibnizOpen
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2012-07-19
1000 Erschienen in
1000 Quellenangabe
  • 287: 33756-33765
1000 FRL-Sammlung
1000 Verlagsversion
  • https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3460472/ |
  • http://doi.org/10.1074/jbc.M112.390849 |
1000 Ergänzendes Material
  • http://www.jbc.org/content/287/40/33756/suppl/DC1 |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • Binding of heterochromatin protein 1 (HP1) to the histone H3 lysine 9 trimethylation (H3K9me3) mark is a hallmark of establishment and maintenance of heterochromatin. Although genetic and cell biological aspects have been elucidated, the molecular details of HP1 binding to H3K9me3 nucleosomes are unknown. Using a combination of NMR spectroscopy and biophysical measurements on fully defined recombinant experimental systems, we demonstrate that H3K9me3 works as an on/off switch regulating distinct binding modes of hHP1β to the nucleosome. The methyl-mark determines a highly flexible and very dynamic interaction of the chromodomain of hHP1β with the H3-tail. There are no other constraints of interaction or additional multimerization interfaces. In contrast, in the absence of methylation, the hinge region and the N-terminal tail form weak nucleosome contacts mainly with DNA. In agreement with the high flexibility within the hHP1β-H3K9me3 nucleosome complex, the chromoshadow domain does not provide a direct binding interface. Our results report the first detailed structural analysis of a dynamic protein-nucleosome complex directed by a histone modification and provide a conceptual framework for understanding similar interactions in the context of chromatin.
  • CAPSULE: BACKGROUND: Chromatin-HP1 (heterochromatin protein 1) interaction is crucial for heterochromatin assembly. RESULTS: hHP1β uses alternative interfaces to bind nucleosomes depending on histone 3 methylation within a highly dynamic complex. CONCLUSION: hHP1β explores chromatin for sites of methyl-mark enrichment where it can bind histone 3 tails from adjacent nucleosomes. SIGNIFICANCE: We provide a conceptual framework to understand the molecular basis of dynamic interactions regulated by histone modification.
1000 Sacherschließung
lokal Heterochromatin
lokal Histone Methylation
lokal NMR
lokal Dynamics
lokal Structural Biology
lokal Epigenetics
lokal Chromatin Regulation
1000 Fachgruppe
  1. Biologie |
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://frl.publisso.de/adhoc/creator/TXVuYXJpLCBGcmFuY2VzY2E=|https://frl.publisso.de/adhoc/creator/U29lcm9lcywgU3phYm9sY3M=|https://frl.publisso.de/adhoc/creator/WmVubiwgSGFucyBNaWNoYWVs|https://frl.publisso.de/adhoc/creator/U2Nob21idXJnLCBBZHJpYW4=|https://frl.publisso.de/adhoc/creator/S29zdCwgTmlscw==|https://frl.publisso.de/adhoc/creator/U2NocsO2ZGVyLCBTYWJyaW5h|https://frl.publisso.de/adhoc/creator/S2xpbmdiZXJnLCBSZWJlY2Nh|https://frl.publisso.de/adhoc/creator/UmV6YWVpLUdoYWxlaCwgTmFzcm9sbGFo|https://frl.publisso.de/adhoc/creator/U3TDvHR6ZXIsIEFsZXhhbmRyYQ==|https://frl.publisso.de/adhoc/creator/R2VsYXRvLCBLYXRoeSBBbm4=|https://frl.publisso.de/adhoc/creator/V2FsbGEsIFBldGVyIEpvbW8=|https://frl.publisso.de/adhoc/creator/QmVja2VyLCBTdGVmYW4=|http://orcid.org/0000-0002-7477-3319|https://frl.publisso.de/adhoc/creator/WmltbWVybWFubiwgQmFzdGlhbg==|https://frl.publisso.de/adhoc/creator/RmlzY2hsZSwgV29sZmdhbmc=|https://frl.publisso.de/adhoc/creator/WndlY2tzdGV0dGVyLCBNYXJrdXM=
1000 Label
1000 Förderer
  1. Max Planck Society |
  2. European Union |
  3. NOE Epigenome |
  4. - |
  5. Deutsche Forschungsgemeinschaft |
1000 Fördernummer
  1. -
  2. -
  3. -
  4. -
  5. ZW 71/2-2; ZW 71/3-2; SFB 860
1000 Förderprogramm
  1. -
  2. Marie Curie reintegration fellowship
  3. NET fellowship
  4. Fonds der Chemischen Industrie
  5. Heisenberg scholarship
1000 Förderung
  1. 1000 joinedFunding-child
    1000 Förderer Max Planck Society |
    1000 Förderprogramm -
    1000 Fördernummer -
  2. 1000 joinedFunding-child
    1000 Förderer European Union |
    1000 Förderprogramm Marie Curie reintegration fellowship
    1000 Fördernummer -
  3. 1000 joinedFunding-child
    1000 Förderer NOE Epigenome |
    1000 Förderprogramm NET fellowship
    1000 Fördernummer -
  4. 1000 joinedFunding-child
    1000 Förderer - |
    1000 Förderprogramm Fonds der Chemischen Industrie
    1000 Fördernummer -
  5. 1000 joinedFunding-child
    1000 Förderer Deutsche Forschungsgemeinschaft |
    1000 Förderprogramm Heisenberg scholarship
    1000 Fördernummer ZW 71/2-2; ZW 71/3-2; SFB 860
1000 Objektart article
1000 Beschrieben durch
1000 @id frl:6403540.rdf
1000 Erstellt am 2017-07-20T07:39:15.784+0200
1000 Erstellt von 25
1000 beschreibt frl:6403540
1000 Bearbeitet von 218
1000 Zuletzt bearbeitet Thu Jan 30 18:02:10 CET 2020
1000 Objekt bearb. Wed Aug 01 12:16:34 CEST 2018
1000 Vgl. frl:6403540
1000 Oai Id
  1. oai:frl.publisso.de:frl:6403540 |
1000 Sichtbarkeit Metadaten public
1000 Sichtbarkeit Daten public
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