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Three-dimensional organization of promyelocytic leukemia nuclear bodies

Promyelocytic leukemia nuclear bodies (PML-NBs) are mobile subnuclear organelles formed by PML and Sp100 protein. They have been reported to have a role in transcription, DNA replication and repair, telomere lengthening, cell cycle control and tumor suppression. We have conducted high-resolution 4Pi...

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Hauptverfasser: Lang, Marion Christine (VerfasserIn) , Jegou, Thibaud (VerfasserIn) , Chung, Inn (VerfasserIn) , Richter, Karsten (VerfasserIn) , Münch, Sandra (VerfasserIn) , Udvarhelyi, Anikó (VerfasserIn) , Cremer, Christoph (VerfasserIn) , Hemmerich, Peter (VerfasserIn) , Engelhardt, Johann (VerfasserIn) , Hell, Stefan (VerfasserIn) , Rippe, Karsten (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 01 February 2010
In: Journal of cell science
Year: 2010, Jahrgang: 123, Heft: 3, Pages: 392-400
ISSN:1477-9137
DOI:10.1242/jcs.053496
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1242/jcs.053496
Volltext
Verfasserangaben:Marion Lang, Thibaud Jegou, Inn Chung, Karsten Richter, Sandra Münch, Anikó Udvarhelyi, Christoph Cremer, Peter Hemmerich, Johann Engelhardt, Stefan W. Hell and Karsten Rippe
Beschreibung
Zusammenfassung:Promyelocytic leukemia nuclear bodies (PML-NBs) are mobile subnuclear organelles formed by PML and Sp100 protein. They have been reported to have a role in transcription, DNA replication and repair, telomere lengthening, cell cycle control and tumor suppression. We have conducted high-resolution 4Pi fluorescence laser-scanning microscopy studies complemented with correlative electron microscopy and investigations of the accessibility of the PML-NB subcompartment. During interphase PML-NBs adopt a spherical organization characterized by the assembly of PML and Sp100 proteins into patches within a 50- to 100-nm-thick shell. This spherical shell of PML and Sp100 imposes little constraint to the exchange of components between the PML-NB interior and the nucleoplasm. Post-translational SUMO modifications, telomere repeats and heterochromatin protein 1 were found to localize in characteristic patterns with respect to PML and Sp100. From our findings, we derived a model that explains how the three-dimensional organization of PML-NBs serves to concentrate different biological activities while allowing for an efficient exchange of components.
Beschreibung:Gesehen am 09.03.2023
Beschreibung:Online Resource
ISSN:1477-9137
DOI:10.1242/jcs.053496

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