Correlation between rDNA transcription and distribution of a 100 kD nucleolar protein in CHO cells

Escande-Géraud, M.L.; Azum, M. C.; Tichadou, J.L.; Gas, Nicole

doi:10.1016/0014-4827(85)90092-8

Cited by 45 publications

(18 citation statements)

References 27 publications

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“…In this regard, Biggiogera et al (4) did not find either a redistribution of B23 protein to the nucleoplasm in the conditions of a physiological diminished rRNA synthesis existing in Golgi phase spermatids. However, our immunocytochemical results are not in accordance with the observations of other authors who have immunolocated the 100 kDa protein on the fibrillar zone of nucleoli where rDNA transcription had been blocked with AMD (19). Likewise, in the case of AMD treatment, our immunolabelling results do not agree with the finding that Ag-NOR proteins have been localized to the fibrillar zone of segregated nucleoli of different types of cells after applying NOR-silver staining (26,27,34,56).…”

Section: Discussioncontrasting

confidence: 99%

“…Protein B23, also called nucleophosmin, N038 or numatrin, is a 36-38 kDa nucleolar phosphoprotein which is more abundant in proliferating than in resting cells, and may be involved in assembly and/or transport of ribosomes (20,46,54). Protein C23, also called nucleolin, is another abundant nucleolar phosphoprotein, with a molecular mass of around 100 kDa, which seems to be involved in the early stages of ribosome biogenesis and to be associated with rDNA-containing structures (19,44,48). The interest in Ag-NOR proteins started with the finding that their amount is directly related to the degree of transcriptional activity, its detection being used as a marker of nucleolar activity and cell proliferation (10,12,15,23,30,34,35,38,40).…”

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An Experimental Approach to the Study of AG-NOR Proteins.

Rodrigo

Maestre

Garcı́a-Herdugo

et al. 1994

Acta Histochem. Cytochem

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Purified polyclonal antibodies have been obtained against 100 KD and 36 KD Ag-NOR proteins. These two antibodies have been used to study the immunolocalization of both proteins on different cell types subjected to various conditions of cell activity and to observe a nucleolar labelling with anti-36 kDa Ag-NOR protein antibody evenly distributed over the dense fibrillar component and granular component, and with anti-100 kDa mainly localized to the dense fibrillar component. After actinomycin D treatment, immunolabelling with both antibodies was found restricted to the granular zone of segregated nucleoli. Moreover, to further study the functional role of these proteins, we have used an electroporation system to introduce both antibodies into the nuclei of living cells, and have clearly detected a different nucleolar behaviour.The combination of these techniques has been shown to be an important tool to deepen the knowledge of the nucleolus and has allowed us to propose that the difference in nucleolar localization of the major 36 kDa and 100 kDa Ag-NOR proteins is the consequence of a different role of both proteins in the synthesis and processing of rRNA.

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Section: Discussioncontrasting

confidence: 99%

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confidence: 99%

An Experimental Approach to the Study of AG-NOR Proteins.

Rodrigo

Maestre

Garcı́a-Herdugo

et al. 1994

Acta Histochem. Cytochem

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“…However, the specific inhibition of RNA polymerase I transcription after nucleolin knockdown by RNA interference (Rickards et al 2007) showed that an important function of nucleolin is to permit RNA polymerase I to transcribe nucleolar chromatin (Rickards et al 2007). Indeed, following inhibition of rRNA transcription, a rapid release of nucleolin from the DFC of the nucleolus was observed (Escande-Geraud et al 1985), demonstrating that its presence in this subnucleolar compartment was dependent upon rRNA transcription. Owing to high structural homology (Ginisty et al 1999), nucleolin can be detected by C23 antibody labeling in many mammalian species.…”

Section: Introductionmentioning

confidence: 99%

Formation of nucleoli in interspecies nuclear transfer embryos derived from bovine, porcine, and rabbit oocytes and nuclear donor cells of various species

Lagutina

Zakhartchenko²,

Fulka³

et al. 2011

Reproduction

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The most successful development of interspecies somatic cell nuclear transfer (iSCNT) embryos has been achieved in closely related species. The analyses of embryonic gene activity in iSCNT embryos of different species combinations have revealed the existence of significant aberrations in expression of housekeeping genes and genes dependent on the major embryonic genome activation (EGA). However, there are many studies with successful blastocyst (BL) development of iSCNT embryos derived from donor cells and oocytes of animal species with distant taxonomical relations (inter-family/inter-class) that should indicate proper EGA at least in terms of RNA polymerase I activation, nucleoli formation, and activation of genes engaged in morula and BL formation. We investigated the ability of bovine, porcine, and rabbit oocytes to activate embryonic nucleoli formation in the nuclei of somatic cells of different mammalian species. In iSCNT embryos, nucleoli precursor bodies originate from the oocyte, while most proteins engaged in the formation of mature nucleoli should be transcribed from genes de novo in the donor nucleus at the time of EGA. Thus, the success of nucleoli formation depends on species compatibility of many components of this complex process. We demonstrate that the time and cell stage of nucleoli formation are under the control of recipient ooplasm. Oocytes of the studied species possess different abilities to support nucleoli formation. Formation of nucleoli, which is a complex but small part of the whole process of EGA, is essential but not absolutely sufficient for the development of iSCNT embryos to the morula and BL stages.

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“…The amount of nucleolin in the cell is correlated directly with nucleolar transcriptional activity (Escande-G6raud et al 1985;Bouche et al 1987). It has been shown to be associated with pre-rRNA {Bugler et al 1987}, chromatin (Olson and Thompson 1983;Erard et al 1988), preribosomes {Bugler et al 1982Herrera and Olson 1986), and the nucleolar matrix and could play a role m the organization of nucleolar substructure.…”

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Nucleolin from Xenopus laevis: cDNA cloning and expression during development.

Caizergues‐Ferrer¹,

Mariottini²,

Curie³

et al. 1989

Genes Dev.

102

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Nucleolin is a key nucleolar protein in higher eukaryotic cells and is involved directly in ribosome biogenesis. Using an antiserum raised against hamster nucleolin, the homologous protein was detected in nucleoli of Xenopns laevis hepatocytes as well as in the amplified nucleoli of oocytes. A cDNA encoding Xenopus nucleolin has been isolated and sequenced. The deduced protein sequence reveals similar domains in Xenopas and in mammals, but they have undergone separate evolutions. In particular, each of the four RNA-binding domains has evolved differentlymthe carboxy-proximal domain is twice as conserved (87%J as the aminoproximal domain (42%). These data shed some light on the possible roles of each domain. The expression of nucleolin has been followed throughout oogenesis and embryogenesis. The appearance of nucleolin during early development precedes the transcription of rDNA and the synthesis of ribosomal proteins. The maximal accumulation of nucleolin at gastrulation coincides with nucleolar reformation. Furthermore, when ribosomal synthesis is activated during oogenesis and embryogenesis, peptides immunorelated to nucleolin appear and accumulate. The results suggest that nucleolin plays a role not only in ribosome assembly but also in nucleologenesis.

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Correlation between rDNA transcription and distribution of a 100 kD nucleolar protein in CHO cells

Cited by 45 publications

References 27 publications

An Experimental Approach to the Study of AG-NOR Proteins.

An Experimental Approach to the Study of AG-NOR Proteins.

Formation of nucleoli in interspecies nuclear transfer embryos derived from bovine, porcine, and rabbit oocytes and nuclear donor cells of various species

Nucleolin from Xenopus laevis: cDNA cloning and expression during development.

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