A Nonribosomal Landscape in the Nucleolus Revealed by the Stem Cell Protein Nucleostemin
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Published:2005-07
Issue:7
Volume:16
Page:3401-3410
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ISSN:1059-1524
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Container-title:Molecular Biology of the Cell
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language:en
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Short-container-title:MBoC
Author:
Politz Joan C. Ritland1, Polena Ilvin1, Trask Ian1, Bazett-Jones David P.2, Pederson Thoru1
Affiliation:
1. Department of Biochemistry and Molecular Pharmacology and Program in Cell Dynamics, University of Massachusetts Medical School, Worcester, MA 01605 2. Program in Cell Biology, Hospital for Sick Children, Toronto, Ontario M5G 1XB, Canada
Abstract
Nucleostemin is a p53-interactive cell cycle progression factor that shuttles between the nucleolus and nucleoplasm, but it has no known involvement in ribosome synthesis. We found the dynamic properties of nucleostemin differed strikingly from fibrillarin (a protein directly involved in rRNA processing) both in response to rRNA transcription inhibition and in the schedule of reentry into daughter nuclei and the nucleolus during late telophase/early G1. Furthermore, nucleostemin was excluded from the nucleolar domains in which ribosomes are born—the fibrillar centers and dense fibrillar component. Instead it was concentrated in rRNA-deficient sites within the nucleolar granular component. This finding suggests that the nucleolus may be more subcompartmentalized than previously thought. In support of this concept, electron spectroscopic imaging studies of the nitrogen and phosphorus distribution in the nucleolar granular component revealed regions that are very rich in protein and yet devoid of nucleic acid. Together, these results suggest that the ultrastructural texture of the nucleolar granular component represents not only ribosomal particles but also RNA-free zones populated by proteins or protein complexes that likely serve other functions.
Publisher
American Society for Cell Biology (ASCB)
Subject
Cell Biology,Molecular Biology
Reference46 articles.
1. Alavian, C. N., Politz, J.C.R., Lewandowski, L. B., Powers, C. M., and Pederson, T. (2004). Nuclear export of signal recognition particle RNA in mammalian cells. Biochem. Biophys. Res. Commun. 313, 351–355. 2. Andersen, J. S., Lyon, C. E., Fox, A. H., Leung, A.K.L., Lam, Y. W., Steen, H., Mann, M., and Lamond, A. I. (2002). Directed proteomic analysis of the human nucleolus. Curr. Biol. 12, 1–11. 3. Bazett-Jones, D. P., Hendzel, M. J., and Kruhlak, M. J. (1999). Stoichiometric analysis of protein- and nucleic acid-based structures in the cell nucleus. Micron 30, 151–157. 4. Borden, K.L.B. (2002). Pondering the promyelocytic leukemia protein (PML) puzzle: possible function for PML nuclear bodies. Mol. Cell. Biol. 22, 5259–5269. 5. Bubulya, P. A., Prasanth, K. V., Deerinck, T. J., Gerlich, D., Beaudouin, J., Ellisman, M. H., Ellenberg, J., and Spector, D. L. (2004). Hypophosphorylated SR splicing factors transiently localize around active nucleolar organizing regions in telophase daughter nuclei. J. Cell Biol. 167, 51–63.
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