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PubMed2000

Immunolocalization of human p14(ARF) to the granular component of the interphase nucleolus.

The human p14(ARF) protein is encoded by an alternative transcript from the INK4a/ARF locus on chromosome 9p21, a locus frequently afflicted in human tumors. By use of two novel specific antisera against p14(ARF) we show that the protein is localized mainly in nucleoli but also in the nucleoplasm. Transfection of full-length and deletion mutant GFP-p14(ARF) fusion proteins confirmed this subcellular localization and assigned the nucleolar localization signal to the exon 2-encoded C-terminal region. In order to determine p14(ARF) expression in human tumor cells, we examined p14(ARF) in 32 tumor cell lines by immunofluorescence staining. Nucleolar p14(ARF) was detected in 10 lines, all of which lacked functional p53. Double immunostaining with p14(ARF) and B23/nucleophosmin or fibrillarin antibodies using 3D microscopy revealed that p14(ARF) is located mainly in the granular component of the nucleolus. p14(ARF) was also found in distinct granular aggregates scattered throughout the nucleoplasm. RNase digestion or selective inhibition of rRNA transcription by low doses of actinomycin D caused nucleoplasmic translocation of p14(ARF). This indicates that the nucleolar localization of p14(ARF) is dependent on ongoing transcriptional activity in intact functional nucleoli.

Animals↗
PubMed2001

Heterochromatin is not an adequate explanation for close proximity of interphase chromosomes 1--Y, 9--Y, and 16--Y in human spermatozoa.

Analysis of human spermatozoa and lymphocytes using C-banding techniques and in situ hybridization has shown a higher order packaging of the human genome. Chromosomes are not distributed entirely at random within the nucleus. In particular, chromosomes 1, 9, and 16, carrying large blocks of pericentromeric heterochromatin, and the Y chromosome, carrying heterochromatin in Yq12, are in close proximity to each other within the nucleus and are involved in somatic pairing with nonhomologous chromosomes. In order to determine whether the close proximity of these chromosomes in any way is attributable to the distribution of heterochromatin, double in situ hybridization was performed on chromosomes 1--Y, 9--Y, and 16--Y as well as on 1--X, 9--X, and 16--X-with chromosome X as the other gonosome carrying less heterochromatin-in human spermatozoa. Each pair was found to have a nonrandom spatial distribution. However, comparison of the arrangement of chromosomes 1--Y versus 1--X and 9--Y versus 9--X revealed that heterochromatin cannot be the only cause for the tendency of chromosome fusion, because only the results of the chromosome pair 1--Y/1--X could support this proposition. In conclusion, the heterochromatin effect cannot be, in itself, an adequate explanation for chromosome association, implicating as well other mechanisms.

Cell Nucleus↗
PubMed2000

Review: dynamic stability of the interphase nucleus in health and disease.

Ongoing export of newly synthesized RNAs, as well as control of transcriptional activity, involves dynamic nucleocytoplasmic transport of proteins. Some proteins that shuttle reside primarily in the nucleus while others are concentrated in the cytoplasm. Moreover, some proteins shuttle continuously, while others shuttle only once. A third group is stimulated to relocate either into or out of the nucleus as a result of interruption of shuttling. In addition to these protein-specific events, several physiological stimuli have global effects on nucleocytoplasmic transport. In related events, selected proteins move between distinct sites in the nucleoplasm, others enter and leave the nucleolus, and still others transit between the nuclear envelope and cytoplasmic membranes. These multiple dynamic distributions provide numerous opportunities for precise communication between spatially distant sites in the cell.

Animals↗
PubMed1997

Ligation-mediated PCR for chromatin-structure analysis of interphase and metaphase chromatin.

Chromatin structure is becoming increasingly recognized as important for a full understanding of gene function and cell memory. With regard to cell memory, which involves the transfer of chromatin-encoded epigenetic information from one cell generation to another, the detailed structure of metaphase chromatin is of crucial importance. In this paper we describe methods for the use of dimethyl sulfate, DNase I, and potassium permanganate for in vivo footprinting and chromatin analysis, with special emphasis on studies of metaphase cells. We review the use of ligation-mediated PCR for the analysis of chromatin, including the human phosphoglycerate kinase promoter, and also report initial studies of a matrix attachment region near the human beta-interferon gene.

Cell Line↗
PubMed1999

Dynamics and mobility of nuclear envelope proteins in interphase and mitotic cells revealed by green fluorescent protein chimeras.

Understanding how membrane proteins are targeted to and retained within the nuclear envelope (NE) and the fate of these proteins during NE disassembly/reassembly in mitosis is central for insight into the function of the NE in nuclear organization and dynamics. To address these issues we have attached green fluorescent protein (GFP) to a well-characterized protein of the inner nuclear membrane, lamin B receptor, believed to be one of the major chromatin docking protein in the NE. We have used this construct in a variety of applications, including dual-color GFP time-lapse imaging, to investigate the mechanisms underlying protein targeting to the NE and NE breakdown and reassembly during mitosis. In this review, we present a summary of the results from such studies and discuss the photobleaching and imaging methodology on which they were derived.

Animals↗
PubMed1995

The role of the Ran GTPase pathway in cell cycle control and interphase nuclear functions.

Ran is a small, highly abundant, nuclear GTPase. Mutants in Ran and in proteins that interact with it disrupt the normal checkpoint control of mitosis with respect to the completion of DNA synthesis. Ran and other components of this pathway are also required for numerous nuclear functions such as RNA export, protein import, RNA processing and DNA replication. It will be important to understand how these facets of Ran's activities are linked and how they promote correct control of the cell cycle. This review examines recent progress in discovering other components of the Ran GTPase pathway and considers how this pathway may be required for the control of the cell cycle.

Cell Cycle↗
PubMed1984

Nucleolus and large nucleolar aggregates of condensed chromatin in interphase nuclei of L 929 cells.

Three-dimensional reconstructions show that the nucleoli from L 929 cells are associated with one or several large aggregates of chromatin displaying a honeycomb-like structure. The form and the number of both nucleoli and honeycomb structures vary as the cells emerge from the resting state and enter exponential growth. Quantitative data show that the number of honeycomb structures decreases as the number of nucleoli diminishes; both numerical regressions are significant. In addition, the nucleoli and the honeycomb structures enlarge when the cells enter the exponential growth phase. In resting cells the number of honeycomb structures is correlated to the number of nucleoli. Therefore we conclude that the large nucleolar mass of condensed chromatin, which in L 929 cells displays a honeycomb structure, contains a portion of the nucleolar organizing region.

Animals↗
PubMed1989

Bent DNA is a structural feature of scaffold-attached regions in Drosophila melanogaster interphase nuclei.

In this study the SAR DNA (scaffold attached region DNA) of some Drosophila genes was analyzed. Bent DNA regions were found to be present in all SAR DNA fragments analyzed here. Bent non-SAR DNA exhibits SAR-like properties when it is exogenously added to lithium 3,5-di-iodosalicylate-extracted Drosophila nuclear scaffolds. Thus the presence of bent regions within SAR DNA fragments might be a prerequisite for the SAR-like behavior of a DNA fragment.

Animals↗
PubMed1981

Further studies on the cytochemistry of the standardized silver staining of interphase nucleoli in smear preparations of Yoshida ascitic sarcoma cells in rats.

Silver staining procedure for the selective demonstration of nucleolar silver stained granules (SSG) and for the simultaneous demonstration of SSG and nucleolar silver stained matrix (SSM) were studied in smears of rat Yoshida sarcoma cells. The successful results of these procedures depend mainly on the quality of silver nitrate and formaldehyde. However, both chemicals can be easily standardized and stabilized disregarding their origin and batch. In standardized procedures (one-step procedure for the selective demonstration of SSG and two-steps procedure for the simultaneous demonstration of SSG and SSM) the silver is apparently bound to acidic groups of proteins of SSG and SSM. The proteins of SSG and SSM seem to be different but both belong to the group of acidic non-histone proteins. According to the results of digestion experiments a possibility also exists that the acidic proteins of SSG may be associated with DNA. The identification of SSG visualized by described standardized procedures was determined not only by cytochemical extraction tests but also by biological experiments. The latter demonstrated that the number of SSG in Yoshida sarcoma cells decreases after treatment of experimental animals with actinomycin D and therefore depends on the state of the nucleolar RNA synthesis.

Animals↗