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Nucleolus

About: Nucleolus is a research topic. Over the lifetime, 5873 publications have been published within this topic receiving 232435 citations. The topic is also known as: GO:0005730 & cell nucleolus.


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Journal ArticleDOI
22 Jan 1971-Science
TL;DR: In wild-type Drosophila melanogaster females there are about 250 ribosomal RNA genes in each nucleolus organizer region of the two X chromosomes, but when this same nucleolUS organizer region is present in flies in only a single dose, the number of ribosome RNA genes increases to approximately 400.
Abstract: In wild-type Drosophila melanogaster females there are about 250 ribosomal RNA genes in each nucleolus organizer region of the two X chromosomes. When this same nucleolus organizer region is present in flies in only a single dose, the number of ribosomal RNA genes increases to approximately 400. This increase is most easily explained by disproportionate replication of these genes.

157 citations

Journal ArticleDOI
TL;DR: It is demonstrated that all of these snRNAs are widespread throughout the nucleoplasm, but they are excluded from the nucleoli, and simultaneous visualization of the U2snRNAs and the tandemly repeated U2 genes demonstrates that coiled bodies are not the sites of U2 transcription.
Abstract: The organization of eight small nuclear ribonucleoproteins (the U1, U2, U4, U5, and U6 RNAs previously studied by others and three additional snRNAs, U11, U12, and 7SK) has been investigated in cultured human cells by fluorescence in situ hybridization with antisense DNA and 2'-O-Me RNA oligonucleotides. Using highly sensitive digital imaging microscopy we demonstrate that all of these snRNAs are widespread throughout the nucleoplasm, but they are excluded from the nucleoli. In addition, the U2, U4, U5, U6, and U12 snRNAs are concentrated in discrete nuclear foci, known as coiled bodies, but U1 and 7SK are not. In addition to coiled bodies, a classic speckled pattern was observed in the nucleoplasm of monolayer-grown HeLa cells, whereas suspension-grown HeLa cells revealed a more diffuse nucleoplasmic labeling. Immunofluorescence staining using various snRNP-specific antisera shows complete agreement with that of their antisense snRNA oligonucleotide counterparts. Although U2 RNA is concentrated in coiled bodies, quantitation of the fluorescence signals from the U2 antisense probe reveals that the bulk of the U2 snRNP is located in the nucleoplasm. Furthermore, simultaneous visualization of the U2 snRNAs and the tandemly repeated U2 genes demonstrates that coiled bodies are not the sites of U2 transcription.

157 citations

Journal ArticleDOI
TL;DR: Beginning at the 8-cell stage, re-incubation in nonradioactive medium results in a significant decrease in nucleolar labeling and an increase in cytoplasmic labeling suggesting that more ribosomal RNA is transferred from the nucleus to the cy toplasm at the later cleavage stages.
Abstract: Studies of cleavage stage mouse embryos are reported, with particular emphasis upon nucleolar fine structural and functional changes. Multiple fibrillar primary nucleoli are present in the early 2-cell embryo. In late 2-cell embryos, some of these nucleoli acquire a peripheral zone of granules, while others reticulate, forming nucleoli composed of fibrillo-granular cortices and fibrillar cores. The nucleoli of early 4-cell embryos are composed only of fibrils. In the middle of the 4-cell stage, some of the nucleoli acquire a peripheral granular zone, while others reticulate. The reticulated nucleoli of both the late 2-cell and 4-cell embryos can be considered, on the basis of their fine structure, to be definitive nucleoli. Early 8-cell and morula embryos usually contain only two definitive nucleoli per nucleus. 3H-5-uridine-pulsed embryos contain label localized in the nucleus, particularly over definitive nucleoli. Nucleolar labeling increases at each successive developmental stage. Beginning at the 8-cell stage, re-incubation in nonradioactive medium results in a significant decrease in nucleolar labeling and an increase in cytoplasmic labeling suggesting that more ribosomal RNA is transferred from the nucleus to the cytoplasm at the later cleavage stages.

156 citations

Journal ArticleDOI
TL;DR: It is reported that a 15-kDa cellular protein called EAP (for EBER associated protein), previously shown to bind EBER1, is in fact the ribosomal protein L22, and in situ hybridization indicates that the EBER RNPs are predominantly nucleoplasmic, suggesting that L22 relocalization correlates with binding to Eber1 in vivo.
Abstract: Epstein-Barr virus (EBV), an oncogenic herpesvirus, encodes two small RNAs (EBERs) that are expressed at high levels during latent transformation of human B lymphocytes Here we report that a 15-kDa cellular protein called EAP (for EBER associated protein), previously shown to bind EBER1, is in fact the ribosomal protein L22 Approximately half of the L22 in EBV-positive cells is contained within the EBER1 ribonucleoprotein (RNP) particle, whereas the other half residues in monoribosomes and polysomes Immunofluorescence with anti-L22 antibodies demonstrates that L22 is localized in the cytoplasm and the nucleoli of uninfected human cells, as expected, whereas EBV-positive lymphocytes also show strong nucleoplasmic staining In situ hybridization indicates that the EBER RNPs are predominantly nucleoplasmic, suggesting that L22 relocalization correlates with binding to EBER1 in vivo Since incubation of uninfected cell extracts with excess EBER1 RNA does not remove L22 from preexisting ribosomes, in vivo binding of L22 by EBER1 may precede ribosome assembly The gene encoding L22 has recently been identified as the target of a chromosomal translocation in certain patients with leukemia, suggesting that L22 levels may be a determinant in cell transformation

156 citations

Journal ArticleDOI
TL;DR: In this article, the authors used mutational analysis, transient transfections, and the yeast two-hybrid system to show that the nucleolar phosphoprotein Nopp140 functions as a molecular link between the two prominent nuclear organelles.
Abstract: Coiled bodies are small nuclear organelles that are highly enriched in small nuclear RNAs, and that have long been thought to be associated with the nucleolus. Here we use mutational analysis, transient transfections, and the yeast two-hybrid system to show that the nucleolar phosphoprotein Nopp140 functions as a molecular link between the two prominent nuclear organelles. Exogenous Nopp140 accumulated in the nucleolus rapidly, but only after a lag phase in coiled bodies, suggesting a pathway between the two organelles. The expression of partial Nopp140 constructs exerted dominant negative effects on the endogenous Nopp140 by chasing it and other antigens that were common to both organelles out of the nucleolus. The alternating positively and negatively charged repeat domain of Nopp140 was required for targeting to both organelles. In addition, partial Nopp140 constructs caused formation of novel structures in the nucleoplasm and, in the case of the conserved carboxy terminus, led to the dispersal of coiled bodies. As a final link, we identified the coiled body–specific protein p80 coilin in a yeast two-hybrid screen with Nopp140. The interaction of the two proteins was confirmed by coimmunoprecipitation. Taken together, Nopp140 appeared to shuttle between the nucleolus and the coiled bodies, and to chaperone the transport of other molecules.

156 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023145
2022209
2021143
2020125
2019139
2018121