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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
TL;DR: The pattern of formation of RNA compounds was closely similar in the two nucleolar organizers and appears to be precursors to 28 and 18 s ribosomal cytoplasmic RNA.

75 citations

Journal ArticleDOI
Nancy J. Lane1
TL;DR: In maturing oocytes of the newt Triturus viridescens, the nucleoli undergo a series of morphological changes that are very similar to those described by Callan for the axolotl, Ambystoma mexicanum.
Abstract: In maturing oocytes of the newt Triturus viridescens, the nucleoli undergo a series of morphological changes that are very similar to those described by Callan for the axolotl, Ambystoma mexicanum. The nucleoli first assume the form of spheroids which then become extended into ring or necklace shapes that are DNase-sensitive; in mature oocytes the nucleoli revert to a spheroidal form. Short term in vitro incorporation studies with uridine-3H on both species show that RNA synthesis occurs in a restricted, eccentric portion of the spheroidal nucleoli, thereby producing an asymmetrical pattern of labeling. In the ring forms, however, the localization of the radioactivity suggests that synthesis takes place symmetrically throughout their entire length. The changes in nucleolar morphology apparently reflect the fact that the component DNA has undergone a redistribution from a localized region in the spheroidal nucleoli to an extended circle in the rings; the patterns of uridine-3H incorporation, therefore, parallel the distribution of DNA in both the spheroidal and the ring nucleoli. Ultrastructurally, the nucleoli contain a fibrillar component that corresponds in position to that of the DNA. The typical spheroidal nucleolus consists of a fibrillar core situated eccentrically and surrounded by a hull of granular, ribonucleoprotein material. The ring nucleoli are composed of a central fibrous region that is ensheathed all around its circumference by a layer of similar granular material. This granular substance is thicker at intervals along the length of the rings, representing the "beads" of the necklaces.

75 citations

Journal ArticleDOI
TL;DR: It is shown that changing parameters as critical as the tandem organization of the ribosomal genes and the polymerase transcribing rDNA, although profoundly modifying the position and the shape of the nucleolus, only partially alter its functional subcompartmentation.
Abstract: Using Saccharomyces cerevisiae strains with genetically modified nucleoli, we show here that changing parameters as critical as the tandem organization of the ribosomal genes and the polymerase transcribing rDNA, although profoundly modifying the position and the shape of the nucleolus, only partially alter its functional subcompartmentation. High-resolution morphology achieved by cryofixation, together with ultrastructural localization of nucleolar proteins and rRNA, reveals that the nucleolar structure, arising upon transcription of rDNA from plasmids by RNA polymerase I, is still divided in functional subcompartments like the wild-type nucleolus. rRNA maturation is restricted to a fibrillar component, reminiscent of the dense fibrillar component in wild-type cells; a granular component is also present, whereas no fibrillar center can be distinguished, which directly links this latter substructure to rDNA chromosomal organization. Although morphologically different, the mininucleoli observed in cells transcribing rDNA with RNA polymerase II also contain a fibrillar subregion of analogous function, in addition to a dense core of unknown nature. Upon repression of rDNA transcription in this strain or in an RNA polymerase I thermosensitive mutant, the nucleolar structure falls apart (in a reversible manner), and nucleolar constituents partially relocate to the nucleoplasm, indicating that rRNA is a primary determinant for the assembly of the nucleolus.

75 citations

Journal ArticleDOI
TL;DR: Active RNA polymerase I appears to be required for the formation of the nucleolus as its major component, and DNA topoisomerases appear to berequired for the folding of rDNA and RNA polymerases I molecules into the functional organization of nucleolar genes.
Abstract: A temperature-sensitive lethal mutant nuc1-632 of Schizosaccharomyces pombe shows marked reduction in macromolecular synthesis and a defective nuclear phenotype with an aberrant nucleolus, indicating a structural role of the nuc1+ gene product in nucleolar organization. We cloned the nuc1+ gene by transformation and found that it appears to encode the largest subunit of RNA polymerase I. We raised antisera against nuc1+ fusion polypeptides and detected a polypeptide (approximately 190 kD and 2 x 10(4) copies/cell) in the S. pombe nuclear fraction. By immunofluorescence microscopy, anti-nuc1+ antibody revealed intense staining at a particular nuclear domain previously defined as the nucleolus. The nucleolar immunofluorescence by anti-nuc1+ was faded in nuc1-632 at restrictive temperature and dramatically diminished in the absence of DNA topoisomerases I and II. Thus active RNA polymerase I appears to be required for the formation of the nucleolus as its major component, and DNA topoisomerases appear to be required for the folding of rDNA and RNA polymerase I molecules into the functional organization of nucleolar genes.

75 citations

Journal ArticleDOI
06 Jan 2000-Oncogene
TL;DR: It is shown that soluble, non-bound p53 is released by permeabilization, leaving structurally bound p53 in both the nucleus and nucleolus, which may explain how relatively few p53 protein molecules can monitor genetic stress and respond preferentially to damage of actively transcribed genes.
Abstract: The p53 tumour suppressor functions as a sensor of genotoxic stress and, once activated, induces cell growth arrest or apoptosis. The precise intranuclear localization of latent p53 protein in non-stressed cells is unknown. Such information is essential in order to understand how relatively few molecules of p53 can detect and respond to DNA damage. Here we present the first detailed supramolecular localization of p53 in the nuclei of cells under normal conditions of growth. We show that soluble, non-bound p53 is released by permeabilization, leaving structurally bound p53 in both the nucleus and nucleolus. In situ biochemical studies reveal (i) that nuclear-bound p53 is tethered by RNA (directly or indirectly) and (ii) that a sub-population of nuclear-bound p53 co-localizes with sites of RNA synthesis. Transcriptional co-localization appeared to be independent of p53 conformation but dependent upon its quaternary structure. In the nucleolus p53 was observed at sites of rRNA synthesis and also adjacent to such sites. In contrast, nucleolar hdm-2 (shown by others to complex p53 and 5S RNA) was excluded from sites of rRNA synthesis. Our discovery that p53 is physically linked with sites of transcription may explain how relatively few p53 protein molecules can monitor genetic stress and respond preferentially to damage of actively transcribed genes.

75 citations


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