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MBC in Press, published online ahead of print April 6, 2005
Mol. Biol. Cell 10.1091/mbc.E05-01-0041

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Submitted on January 19, 2005
Revised on March 18, 2005
Accepted on March 24, 2005

Tracking the Interactions of rRNA Processing Proteins during Nucleolar Assembly in Living Cells

Nicole Angelier,* Marc Tramier,{dagger} Emilie Louvet,* Maïté Coppey-Moisan,{dagger} Tula M. Savino,* Jan R. De Mey,{ddagger} and Danièle Hernandez-Verdun D*

*Nuclei and Cell Cycle Laboratory and {dagger}Macromolecular Complexes in Live Cells, Institut Jacques Monod, CNRS, University Paris VI and Paris VII, 75251 Paris, France; {ddagger}Microtubules and Morphogenesis Laboratory, ESBS, University Louis Pasteur, CNRS UMR 7100, 67400 Illkirch-Graffenstaden, France

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 4D imaging and quantification, while a different order of processing protein recruitment into nucleoli is supported by differential sorting. Protein interactions along the recruitment pathway was investigated using a promissing 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 suggest that PNBs are preassembly platforms for rRNA processing complexes.

Address correspondence to: Danièle Hernandez-Verdun D (dhernand{at}ccr.jussieu.fr)




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