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At least 127 records · Page 7Linked to original sources
PubMed1995

mRNA transport in yeast: time to reinvestigate the functions of the nucleolus.

Nucleocytoplasmic transport of mRNA is vital to gene expression and may prove to be key to its regulation. Genetic approaches in Saccharomyces cerevisiae have led to the identification of conditional mutants defective in mRNA transport. Mutations in approximately two dozen genes result in accumulation of transcripts, trapped at various sites in the nucleus, as detected by in situ hybridization. Phenotypic and molecular analyses of many of these mRNA transport mutants suggest that, in yeast, the function of the nucleus is not limited to the biogenesis of pre-ribosomes but may also be important for transport of poly(A)+ RNA. A similar function of the animal cell nucleolus is suggested by several observations.

Animals↗
PubMed1993

Nucleolar targeting signal of Rex protein of human T-cell leukemia virus type I specifically binds to nucleolar shuttle protein B-23.

Rex protein, the post-transcriptional regulator of human T-cell leukemia virus type I, is located predominantly in the cell nucleolus and is associated with the cytoplasmic accumulation of unspliced and singly spliced viral mRNAs. The N-terminal 19-amino acid segment of Rex has been identified as the nucleolar targeting signal (NOS) and shown to be important for Rex function. To study the molecular interaction between the NOS region of Rex and its binding host protein(s) in the nucleolus, we chemically synthesized a functional NOS peptide (wild type) and mutant NOS peptides. Fluorescein isothiocyanate-conjugated functional NOS peptide was rapidly taken up by human cells and was transported to the nucleolus. Using affinity chromatography, we identified nucleolar protein B-23 as the major protein that binds to NOS. We also identified two highly acidic regions of B-23 (amino acids 120-132 and 161-188) as acceptor regions for NOS. Previous experiments have suggested that B-23 functions as a shuttle protein for the nucleolar transport of ribosomal components. Our results suggest that B-23 may also serve as a shuttle for the import of Rex from the cytoplasm to the nucleolus coupled to the export of viral mRNAs containing the Rex-responsive element.

Amino Acid Sequence↗
PubMedDate not supplied

[Altered gravity affects subnucleolus localization of fibrillarin and NopA64, the most important proteins of rRNA processing].

Fibrillarin and plant nucleolin homologue NopA64 are two important nucleolar proteins involved in pre-rRNA processing. To understand better the effects of the altered gravity environment on the nucleolus functioning we have investigated the location of fibrillarin and NopA64 in nucleolar subcomponents of cress (Lepidium sativum L.) root meristematic cells grown under simulated microgravity that was compared to the control cells grown in normal conditions at I g. Cress fibrillarin was first shown to have the molecular weight 41 kDa. Both fibrillarin and NopA64 in the cress cell nucleolus are located in the zones known to contain processing pre-rRNA molecules as it has been previously reported in other species. The data confirm participation of these proteins in processomes--RNP complex particles involved in pre-rRNA processing. Under altered gravity a decrease in the quantity of both fibrillarin and NopA64 in the transition zone between fibrillar centres and the dense fibrillar component was observed, compared to control, which could point out to a lowering of the level of early pre-rRNA processing in these experimental conditions. This decrease was also detected in the bulk of the dense fibrillar component. These data support the idea that altered (reduced) gravity results in lowering the level of functional activity of the nucleolus.

Cell Nucleolus↗
PubMed1993

Cellular relations in mouse circumvallate taste buds.

The fine structure of the taste buds of circumvallate papillae of two strains of mice was studied by electron microscopy. Mice anesthetized with ketamine were perfused through the heart with a double aldehyde mixture in cacodylate buffer and the tissues embedded in Epon. Semi-serial sections were employed. The morphology and relationships of cell types are consistent with the majority of descriptions of mammalian taste buds served by the ninth cranial nerve. Cells of type II are particularly well documented, as the stages in their origin, maturation and degeneration could be followed. Significant differences, however, relate to cell type I. These cells contain large dense-cored granules, contrasted with the more irregular and somewhat larger dark granules of the type I cells in the rabbit. These granules do not produce a dense homogenous product for the pore, as seen in the rabbit. Rather the pore substance consists of small, empty vesicles in a diffuse dark matrix. These granules are only moderately larger than the dense-cored vesicles of the type III cells. All features of the type III cell were demonstrated, although no instance of a complete cell was seen in any section. No significant differences were noted between the two strains of mice. Intimate proximity of a nerve to a cell nucleolus, suggestive of a trophic pathway, is illustrated.

Animals↗
PubMed1994

Physiologically inactive nucleoli contain nucleoplasmic ribonucleoproteins: immunoelectron microscopy of mouse spermatids and early embryos.

Physiologically inactivating or reactivating nucleoli represent a good model to investigate modifications of the nucleolar activity, which influence to a great extent the morphology of this organelle. We have studied the nucleoli of mouse spermatids during gradual inactivation, as well as those of early mouse preimplantation embryos, which undergo reactivation. In the 2-cell systems, inactive nucleoli are represented by homogeneously, finely fibrillar spherical bodies. With the aim of clarifying the composition of these nucleoli, we have analyzed them by means of immunoelectron microscopy using specific antibodies directed against nucleoplasmic snRNPs, hnRNPs, ribosomal proteins, or fibrillarin as well as by cytochemical methods for visualizing DNA and RNA. Our results indicate that RNA is present in zygote and 2-cell nucleolus precursor bodies (NPBs) as well as in 4- to 8-cell or more advanced embryo nucleoli, but not in inactive spermatid nucleoli. DNA is absent from inactive spermatid nucleoli and NPBs but is present within the nucleolus-associated chromatin and the nucleolonema of active nucleoli. The dense masses constituting the NPBs of the zygote and 2-cell embryos contain ribosomal proteins and fibrillarin but also hnRNPs and nucleoplasmic snRNPs. Of these, only fibrillarin is present in the spermatid residual nucleoli.

Animals↗
PubMed2003

Yeast Nop15p is an RNA-binding protein required for pre-rRNA processing and cytokinesis.

Nop15p is an essential protein that contains an RNA recognition motif (RRM) and localizes to the nucleoplasm and nucleolus. Cells depleted of Nop15p failed to synthesize the 25S and 5.8S rRNA components of the 60S ribosomal subunit, and exonucleolytic 5' processing of 5.8S rRNA was strongly inhibited. Pre-rRNAs co-precipitated with tagged Nop15p confirmed its association with early pre-60S particles and Nop15p bound a pre-rRNA transcript in vitro. Nop15p-depleted cells show an unusually abrupt growth arrest prior to substantial depletion of ribosomal subunits. Following cell synchronization in mitosis, Nop15p-depleted cells undergo nuclear division with wild-type kinetics, activate the mitotic exit network and disassemble their mitotic spindle. However, they uniformly arrest at cytokinesis and fail to assemble a contractile actin ring at the bud neck. In dividing wild-type cells, segregation of nucleolar proteins to the daughter nuclei occurs after separation of the nucleoplasm. In these late mitotic cells, Nop15p was partially delocalized from the nucleolus to the nucleoplasm, consistent with a specific function in cell division in addition to its role in ribosome synthesis.

Base Sequence↗
PubMed1993

Cytotoxic activity of rev protein of human immunodeficiency virus type 1 by nucleolar dysfunction.

The rev protein (Rev) of the human immunodeficiency virus type 1 (HIV-1) is known as a post-transcriptional regulator of viral gene expression. It is located in the cell nucleolus. Transiently expressed Rev caused nucleolar ballooning and deformity with aberrant accumulation of rRNAs, and de novo synthesis of rRNAs decreased dramatically in these cells. However, similarly expressed rex protein (Rex) of the human T-cell leukemia virus type I, which is a functional homologue to Rev, did not affect nucleolar structure and function. Rev expression resulted in cell death with nucleolar destruction in an inducible cell line. Analysis of Rev mutants revealed that both the nucleolar targeting signal of Rev and the multimerization domain are prerequisites to the nucleolar disintegration by Rev. Human T-cells acutely infected with HIV-1 contained nucleoli which were deformed and filled with Rev, but chronically infected cells had intact nucleoli. Involvement of Rev in cytopathic effects in HIV-1 infection is discussed.

Base Sequence↗