ArticleMolecular biology of the cell2005
Tracking the interactions of rRNA processing proteins during nucleolar assembly in living cells.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 72 citations in OpenAlex.
- Elucidating structure-function relationships in the mammalian nucleolus.Nature reviews. Molecular cell biology · 2026Review
- Ribosomal RNA regulates chromosome clustering during mitosis.Cell discovery · 2022Article
- The intrinsically disorderly story of Ki-67.Open biology · 2021Review
- Luminescence lifetime imaging of three-dimensional biological objects.Journal of cell science · 2021Article
- Trnp1 organizes diverse nuclear membrane-less compartments in neural stem cells.The EMBO journal · 2020Article
- Mapping the nucleolar proteome reveals a spatiotemporal organization related to intrinsic protein disorder.Molecular systems biology · 2020Article
- Nucleolar Division in the Promastigote Stage ofBioMed research international · 2018Article
- Cytogenetic analysis and chromosomal characteristics of the polymorphic 18S rDNA of Haliotis discus hannai from Fujian, China.PloS one · 2015Article
- Article
- Nuclear myosin 1c facilitates the chromatin modifications required to activate rRNA gene transcription and cell cycle progression.PLoS genetics · 2013Article
- Nucleologenesis in the Caenorhabditis elegans embryo.PloS one · 2012Article
- The Fate of the Nucleolus during Mitosis: Comparative Analysis of Localization of Some Forms of Pre-rRNA by Fluorescent in Situ Hybridization in NIH/3T3 Mouse Fibroblasts.Acta naturae · 2011Article
- Non fitting based FRET-FLIM analysis approaches applied to quantify protein-protein interactions in live cells.Biophysical reviews · 2011Review
- High-resolution whole-genome sequencing reveals that specific chromatin domains from most human chromosomes associate with nucleoli.Molecular biology of the cell · 2010Article
- Double duty for nuclear proteins--the price of more open forms of mitosis.Trends in genetics : TIG · 2009Review
- Quantitative comparison of different fluorescent protein couples for fast FRET-FLIM acquisition.Biophysical journal · 2009Article
- Nucleolar separation from chromosomes during Aspergillus nidulans mitosis can occur without spindle forces.Molecular biology of the cell · 2009Article
- Old and new faces of the nucleolus. Workshop on the Nucleolus and Disease.EMBO reports · 2009Article
- Viral nucleolar localisation signals determine dynamic trafficking within the nucleolus.Virology · 2008Article
- Quantitative FRET analysis by fast acquisition time domain FLIM at high spatial resolution in living cells.Biophysical journal · 2008Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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