Three-dimensional organization of promyelocytic leukemia nuclear bodies

• Verfasst von: Lang, Marion Christine [VerfasserIn]
• Verfasst von: Jegou, Thibaud [VerfasserIn]
• Verfasst von: Chung, Inn [VerfasserIn]
• Verfasst von: Richter, Karsten [VerfasserIn]
• Verfasst von: Münch, Sandra [VerfasserIn]
• Verfasst von: Udvarhelyi, Anikó [VerfasserIn]
• Verfasst von: Cremer, Christoph [VerfasserIn]
• Verfasst von: Hemmerich, Peter [VerfasserIn]
• Verfasst von: Engelhardt, Johann [VerfasserIn]
• Verfasst von: Hell, Stefan [VerfasserIn]
• Verfasst von: Rippe, Karsten [VerfasserIn]
• Titel: Three-dimensional organization of promyelocytic leukemia nuclear bodies
• Verf.angabe: Marion Lang, Thibaud Jegou, Inn Chung, Karsten Richter, Sandra Münch, Anikó Udvarhelyi, Christoph Cremer, Peter Hemmerich, Johann Engelhardt, Stefan W. Hell and Karsten Rippe
• E-Jahr: 2010
• Jahr: 01 February 2010
• Umfang: 9 S.
• Fussnoten: Gesehen am 09.03.2023
• Titel Quelle: Enthalten in: Journal of cell science
• Ort Quelle: Cambridge : Company of Biologists Limited, 1853
• Jahr Quelle: 2010
• Band/Heft Quelle: 123(2010), 3 vom: Feb., Seite 392-400
• ISSN Quelle: 1477-9137
• DOI: doi:10.1242/jcs.053496
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1838749438

Abstract

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.