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Vol. 16, Issue 6, 2862-2871, June 2005
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* Nuclei and Cell Cycle Laboratory, Institut Jacques Monod, Centre National de la Recherche Scientifique, University Paris VI and Paris VII, 75251 Paris, France;
Macromolecular Complexes in Live Cells, Institut Jacques Monod, Centre National de la Recherche Scientifique, University Paris VI and Paris VII, 75251 Paris, France; and
Microtubules and Morphogenesis Laboratory, Ecole Supérieure de Biotechnologie de Strasbourg, Centre National de la Recherche Scientifique Unité Mixte Recherche 7100, 67400 Illkirch-Graffenstaden, France
Submitted January 19, 2005;
Revised March 18, 2005;
Accepted March 24, 2005
Monitoring Editor: Joseph Gall
Reorganization of the nuclear machinery after mitosis is a fundamental but poorly understood process. Here, we investigate the recruitment of the nucleolar processing proteins in the nucleolus of living cells at the time of nucleus formation. We question the role of the prenucleolar bodies (PNBs), during migration of the processing proteins from the chromosome periphery to sites of rDNA transcription. Surprisingly, early and late processing proteins pass through the same PNBs as demonstrated by rapid two-color four-dimensional imaging and quantification, whereas a different order of processing protein recruitment into nucleoli is supported by differential sorting. Protein interactions along the recruitment pathway were investigated using a promising time-lapse analysis of fluorescence resonance energy transfer. For the first time, it was possible to detect in living cells the interactions between proteins of the same rRNA processing machinery in nucleoli. Interestingly interactions between such proteins also occur in PNBs but not at the chromosome periphery. The dynamics of these interactions suggests that PNBs are preassembly platforms for rRNA processing complexes.
Abbreviations used: DsRed, Discosoma red fluorescence protein; FRET, fluorescence resonance energy transfer; GFP, green fluorescence protein; PNB, prenucleolar body; ROI, regions of interest; tdFLIM, time domain fluorescence lifetime imaging microscopy.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Danièle Hernandez-Verdun (dhernand{at}ccr.jussieu.fr).
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