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1000 Titel
  • Dynamic as well as stable protein interactions contribute to genome function and maintenance
1000 Autor/in
  1. Hemmerich, Peter |
  2. Schmiedeberg, Lars |
  3. Diekmann, Stephan |
1000 Erscheinungsjahr 2010
1000 Art der Datei
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2010-11-03
1000 Erschienen in
1000 Quellenangabe
  • 19(1): 131–151
1000 FRL-Sammlung
1000 Copyrightjahr
  • 2010
1000 Lizenz
1000 Verlagsversion
  • http://dx.doi.org/10.1007/s10577-010-9161-8 |
  • https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3040344/ |
1000 Ergänzendes Material
  • https://static-content.springer.com/esm/art%3A10.1007%2Fs10577-010-9161-8/MediaObjects/10577_2010_9161_MOESM1_ESM.xls |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • The cell nucleus is responsible for the storage, expression, propagation, and maintenance of the genetic material it contains. Highly organized macromolecular complexes are required for these processes to occur faithfully in an extremely crowded nuclear environment. In addition to chromosome territories, the nucleus is characterized by the presence of nuclear substructures, such as the nuclear envelope, the nucleolus, and other nuclear bodies. Other smaller structural entities assemble on chromatin in response to required functions including RNA transcription, DNA replication, and DNA repair. Experiments in living cells over the last decade have revealed that many DNA binding proteins have very short residence times on chromatin. These observations have led to a model in which the assembly of nuclear macromolecular complexes is based on the transient binding of their components. While indeed most nuclear proteins are highly dynamic, we found after an extensive survey of the FRAP literature that an important subset of nuclear proteins shows either very slow turnover or complete immobility. These examples provide compelling evidence for the establishment of stable protein complexes in the nucleus over significant fractions of the cell cycle. Stable interactions in the nucleus may, therefore, contribute to the maintenance of genome integrity. Based on our compilation of FRAP data, we propose an extension of the existing model for nuclear organization which now incorporates stable interactions. Our new “induced stability” model suggests that self-organization, self-assembly, and assisted assembly contribute to nuclear architecture and function.
1000 Sacherschließung
lokal Nucleus
lokal Self-assembly
lokal Induced stability
lokal Residence time
lokal Dynamics
lokal Chromatin binding
lokal FRAP
lokal Multi-protein complex
lokal Assisted assembly
lokal Fluorescence microscopy
lokal Self-organization
1000 Fachgruppe
  1. Medizin |
  2. Gesundheitswesen |
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://frl.publisso.de/adhoc/creator/SGVtbWVyaWNoLCBQZXRlcg==|https://frl.publisso.de/adhoc/creator/U2NobWllZGViZXJnLCBMYXJz|https://frl.publisso.de/adhoc/creator/RGlla21hbm4sIFN0ZXBoYW4=
1000 Label
1000 Förderer
  1. DFG |
  2. BMBF |
1000 Fördernummer
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  2. -
1000 Förderprogramm
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  2. -
1000 Dateien
1000 Förderung
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    1000 Förderer DFG |
    1000 Förderprogramm -
    1000 Fördernummer -
  2. 1000 joinedFunding-child
    1000 Förderer BMBF |
    1000 Förderprogramm -
    1000 Fördernummer -
1000 Objektart article
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1000 @id frl:6403515.rdf
1000 Erstellt am 2017-07-18T11:39:06.236+0200
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1000 Zuletzt bearbeitet Thu Jan 30 20:32:36 CET 2020
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1000 Oai Id
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