Reference : Localization of Nopp140 within mammalian cells during interphase and mitosis.
Scientific journals : Article
Life sciences : Anatomy (cytology, histology, embryology...) & physiology
http://hdl.handle.net/2268/30025
Localization of Nopp140 within mammalian cells during interphase and mitosis.
English
Thiry, Marc mailto [Université de Liège - ULg > Département des sciences de la vie > Biologie cellulaire >]
Cheutin, Thierry [> > > >]
Lamaye, Françoise mailto [Université de Liège - ULg > Département des sciences de la vie > Biologie cellulaire >]
Thelen, Nicolas mailto [Université de Liège - ULg > Département des sciences de la vie > Biologie cellulaire >]
Meier, U Thomas [> > > >]
O'Donohue, Marie*-Francoise [> > > >]
Ploton, Dominique [> > > >]
2009
Histochemistry & Cell Biology
Springer Science & Business Media B.V.
132
2
129-40
Yes (verified by ORBi)
International
0948-6143
1432-119X
New York
NY
[en] Cell Nucleus/metabolism ; Coiled Bodies/metabolism ; Fluorescent Antibody Technique ; Hela Cells ; Humans ; Imaging, Three-Dimensional ; Interphase ; Microscopy, Confocal ; Microscopy, Immunoelectron ; Mitosis ; Nuclear Proteins/analysis/metabolism ; Phosphoproteins/analysis/metabolism ; RNA Precursors/metabolism ; RNA Processing, Post-Transcriptional
[en] We investigated distribution of the nucleolar phosphoprotein Nopp140 within mammalian cells, using immunofluorescence confocal microscopy and immunoelectron microscopy. During interphase, three-dimensional image reconstructions of confocal sections revealed that nucleolar labelling appeared as several tiny spheres organized in necklaces. Moreover, after an immunogold labelling procedure, gold particles were detected not only over the dense fibrillar component but also over the fibrillar centres of nucleoli in untreated and actinomycin D-treated cells. Labelling was also consistently present in Cajal bodies. After pulse-chase experiments with BrUTP, colocalization was more prominent after a 10- to 15-min chase than after a 5-min chase. During mitosis, confocal analysis indicated that Nopp140 organization was lost. The protein dispersed between and around the chromosomes in prophase. From prometaphase to telophase, it was also detected in numerous cytoplasmic nucleolus-derived foci. During telophase, it reappeared in the reforming nucleoli of daughter nuclei. This strongly suggests that Nopp140 could be a component implicated in the early steps of pre-rRNA processing.
http://hdl.handle.net/2268/30025
10.1007/s00418-009-0599-8

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