SEARCH · PubMed Health

Results for “RNA Transport”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources

PubMed1997

RNA transport.

RNA molecules synthesized in the nucleus are transported to their sites of function throughout the eukaryotic cell by specific transport pathways. This review focuses on transport of messenger RNA, small nuclear RNA, ribosomal RNA, and transfer RNA between the nucleus and the cytoplasm. The general molecular mechanisms involved in nucleocytoplasmic transport of RNA are only beginning to be understood. However, during the past few years, substantial progress has been made. A major theme that emerges from recent studies of RNA transport is that specific signals mediate the transport of each class of RNA, and these signals are provided largely by the specific proteins with which each RNA is associated.

Animals↗

PubMed1989

Hybridization analysis of RNA transported from rat liver nuclei in response to 35 kDa normal and 60 kDa messenger RNA transport factors.

The transport of messenger RNA (mRNA) in response to normal adult (35 kDa) and oncofetal (60 kDa) transport factors has been studied in a reconstituted cell-free system. Poly(A)+ mRNA sequences transported by the 35 kDa and 60 kDa transport factors were compared by cDNA:RNA hybridization kinetics. Heterologous hybridization reactions indicated that a proportion of messengers transported in response to the 35 kDa factor were absent or at a markedly reduced abundance in the mRNA released by the 60 kDa factor. Recombinant DNA probes containing cDNA inserts were used to quantitate transport of rat-liver-specific alpha 2 mu-globulin and albumin mRNA from isolated nuclei in presence of the normal and tumor-specific transport factors. More alpha 2 mu-globulin and albumin messenger sequences were transported in response to the 35 kDa transport factor as compared to the 60 kDa factor. These results indicate that the 35 kDa transport protein isolated from rat liver cytosol and the 60 kDa transport protein isolated from hepatoma cytosol, differ significantly in specificity for the classes of RNA sequences released from nuclei. Monoclonal antibodies against the 60 kDa factor do not cross-react with the 35 kDa factor or other proteins as determined by the immunobioassay and by the Western blot technique.

Albumins↗

PubMed1978

Energy utilization and RNA transport: their interdependence.

The interdependence of RNA transport and the metabolism of nucleotide additives was investigated. Rat-liver RNA was radioactively labeled in vivo for 45 min before isolation of liver nuclei, and the concentration dependence of RNA transport on nucleotide additives was determined. In a parrallel investigation, using nucleotide additives labeled in the base moiety, the distributions of label in the tri-, di-, and monophosphate forms were examined after various intervals of incubation. Analysis of results revealed that RNA transport was linearly related to the decline in energy charge of nucleotide additives, whith high statistical correlation. Kinetic analysis of labeled-nucleotide metabolism led to a simple schematic model for pathways for the utilization of high-energy phosphate bonds, and predictions of the scheme were confirmed by studies examining the effects of nucleotide analogues upon RNA transport. Data concerning inhibitors and chelators intimated that multiple avenues of inhibition and stimulation may potentially influence RNA transport. On the basis of previous data and the results presented in this communication, we conclude that nucleocytoplasmic RNA transport is dependent upon high-energy phosphate-bond hydrolysis and that nucleotides do not stimulate RNA transport via a simple chelation mechanism.

Adenine Nucleotides↗

PubMed1977

Effect of temperature on nuclear membranes and nucleo-cytoplasmic RNA-transport in Tetrahymena grown at different temperatures.

The effect of temperature on the nuclear envelope structure and the transport of total RNA and ribosomal subunits from nucleus to cytoplasm was examined in Tetrahymena cells propagated at two different temperatures. Freeze-etch electron microscopy of cells grown at 23 and 18 degrees C detects the emergence of smooth areas on the fracture faces of the nuclear membranes upon lowering the temperature below approximately 15 and approximately 12 degrees C, respectively. Coincident with these freeze-etch changes, a discontinuous decrease is observed in the nucleocytoplasmic RNA-transport; this is probably not due to a cease in RNA-synthesis. Below the thermotropic discontinuity observed in the transport of total RNA in 18 degrees-cells the nucleocytoplasmic transport of the small and large ribosomal subunits is equally retarded. Recent temperature studies on the endoplasmic reticulum membranes of Tetrahymena suggest that the freeze-etch changes in the nuclear membranes are induced by a thermotropic clustering of the membrane lipids. We conclude that this lipid clustering induces the permanent protein constituents in the nuclear envelope pore complexes to change from a relatively "open" into a relatively "closed" state thus causing the observed decrease in RNA-transport.

Biological Transport↗

PubMed1981

RNA metabolism in isolated nuclei: effect of temperature on RNA transport from intact and membrane-denuded nuclei.

The kinetics of RNA transport from intact (both inner and outer nuclear membranes present) and membrane-denuded myeloma nuclei were monitored at temperatures between 10 and 37 degrees C. A linear rate for RNA transport was calculated and the log of RNA transported from membrane-denuded nuclei was greater than that transported from intact nuclei and ii) RNA transport from both nuclear preparations exhibited straight line Arrhenius plots. We conclude the nuclear envelope (or a nuclear matrix element) modulates the amount of RNA transported from nuclei and that nuclear membrane thermal phase transitions do not alter the apparent energy of activation for the transport process.

Animals↗

PubMed1985

Nucleocytoplasmic RNA transport.

A number of closely related post-transcriptional facets of RNA metabolism show nuclear compartmentation, including capping, methylation, splicing reactions, and packaging in ribonucleoprotein particles (RNP). These nuclear 'processing' events are followed by the translocation of the finished product across the nuclear envelope. Due to the inherent complexity of these interrelated events, in vitro systems have been designed to examine the processes separately, particularly so with regard to translocation. A few studies have utilized nuclear transplantation/microinjection techniques and specialized systems to show that RNA transport occurs as a regulated phenomenon. While isolated nuclei swell in aqueous media and dramatic loss of nuclear protein is associated with this swelling, loss of RNA is not substantial, and most studies on RNA translocation have employed isolated nuclei. The quantity of RNA transported from isolated nuclei is related to hydrolysis of high-energy phosphate bonds in nucleotide additives. The RNA is released predominantly in RNP: messenger-like RNA is released in RNP which have buoyant density and polypeptide composition similar to cytoplasmic messenger RNP, but which have distinctly different composition from those in heterogeneous nuclear RNP. Mature 18 and 28S ribosomal RNA is released in 40 and 60S RNP which represent mature ribosomal subunits. RNA transport proceeds with characteristics of an energy-requiring process, and proceeds independently of the presence or state of fluidity of nuclear membranes. The energy for transport appears to be utilized by a nucleoside triphosphatase (NTPase) which is distributed mainly within heterochromatin at the peripheral lamina. Photoaffinity labeling has identified the pertinent NTPase as a 46 kD polypeptide which is associated with nuclear envelope and matrix preparations. The NTPase does not appear to be modulated via direct phosphorylation or to reflect kinase-phosphatase activities. A large number of additives (including RNA and insulin) produce parallel effects upon RNA transport and nuclear envelope NTPase, strengthening the correlative relationship between these activities. Of particular interest has been the finding that carcinogens induce specific, long-lasting increases in nuclear envelope (and matrix) NTPase; this derangement may underlie the alterations in RNA transport associated with cancer and carcinogenesis.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗

PubMed1974

Reversible, thermotropic alteration of nuclear membrane stucture and nucleocytoplasmic RNA transport in Tetrahymena.

We examine the effect of cooling upon the freeze-etch ultrastructure of nuclear membranes, as well as upon nucleocytoplasmic RNA transport in the unicellular eukaryote Tetrahymena pyriformis. Chilling produces smooth, particle-free areas on both faces of the two freeze-fractured macronuclear membranes. Upon return to optimum growth temperature the membrane-associated particles revert to their normal uniform distribution and the smooth areas disappear. Chilling lowers the incorporation of [(14)C]uridine into whole cells and their cytoplasmic RNA. Cooling from the optimum growth temperature of 28 degrees to 18 degrees C (or above) decreases [(14)C]uridine incorporation into cells more than into their cytoplasmic RNA; chilling to below 18 degrees C but above 10 degrees C causes the reverse. [(14)C]Uridine incorporation into whole cells and their cytoplasmic RNA reflects overall RNA synthesis and nucleocytoplasmic RNA transport, respectively. RNA transport decreases strongly between 20 degrees and 16 degrees C, which is also the temperature range where morphologically detectable nuclear membrane transitions occur. This suggests that the nuclear envelope limits the rate of nucleocytoplasmic RNA transport at low temperatures. We hypothesize that a thermotropic lipid phase transition switches nuclear pore complexes from an "open" to a "closed" state with respect to nucleocytoplasmic RNA transport.

Animals↗

PubMed1984

Relationship between the transport from isolated nuclei of two abundant cytoplasmic messengers and the source of a messenger RNA transport factor.

Messenger RNA transport from isolated nuclei requires a 35 X 10(3) dalton cytoplasmic protein(s) which is present in both the cytosol and polyribosome fractions. Recombinant DNA probes containing cDNA inserts were used to quantitate the transport of rat liver-specific albumin and male rat liver-specific alpha 2U-globulin messenger RNA (mRNA) from male rat liver nuclei in response to the mRNA transport factors from homologous and heterologous tissues. No mRNA transport occurs in the absence of the transport factor(s). Both messengers are transported proportionately in response to the factor(s) from male or female rat liver cytosol, or from the polyribosomes (messenger ribonucleoprotein) of male or female rat liver, or brain. The transport factor(s) do not, therefore, appear to differentiate between the coding sequences of two unrelated hepatic messenger RNA's.

Albumins↗

PubMed1977

RNA transport in the embryonic cell.

The modern data on RNA transport in the cells of early embryos are reviewed. A special attention is paid to the specificity of posttranscriptional mRNA transformation and the control of its transport from the nucleus to the cytoplasm. These processes in the embryonic cell differ from those in the adult one: in the embryos the rate of transport of mRNA molecules in the cytoplasm increases with the development (with the onset of gastrulation); the process of polyadenylation in some mRNA molecules takes place in the cytoplasm rather than in the nucleus; besides, the high molecular weight mRNA fractions are localized in the cytoplasm (in the adult cells they are found only in the nucleus). A study of the mechanisms of control of mRNA transport from the nucleus in the cytoplasm has shown that the now existing concepts on the participation of nucleolus, as well as of translation mechanisms in the control of mRNA transport appear to be true only for the differentiated cells and cannot be used to account for the control of mRNA transport in the embryos. For the embryonic cells the hypothesis on the selection of populations of mRNA molecules at the level of transport for their entry into the cytoplasm holds true. The patterns of RNA transport during the cell division are also considered, with respect to the phenomenon of migration of some RNA populations synthesized prior to the onset of division in the nuclei of daughter cells.

Animals↗

PubMed1986

Quantitative ultrastructural autoradiographic study of RNA transport in rat ventral prostate.

The nucleocytoplasmic RNA transport in rat ventral prostate was studied by electron microscope autoradiography. Isolated prostate acini from normal, castrated, and DHT-treated animals were labeled in vitro with [3H]uridine for 5 min and chased for 0, 15, 30 min and 4 hr. The results show that DHT induces a significant nucleolar enlargement but intranuclear migration of rRNA is not apparently affected by androgens; migration of RNA through euchromatin is delayed by castration and stimulated by DHT; migration through the nuclear envelope is androgen-dependent. In addition prostate acini were maintained for 24 hr in suspension culture in order to study the in vitro effects of DHT. The result show that DHT stimulates uridine uptake and/or incorporation but induces no nucleolar enlargement; DHT has no clear effects on RNA migration kinetics; cytoplasmic transport of RNA in cells cultured in medium with or without DHT is severely impaired but is restored after supplementation of medium with insulin and dexamethasone.

Animals↗

PubMed2002

The nuclear connection in RNA transport and localization.

RNA-binding proteins are involved in various aspects of RNA metabolism such as processing, translational control, stabilization, localization and transport. Many of these proteins bind several RNA targets and have multiple functions. In this review we focus on RNA-binding proteins that are implicated in RNA transport and localization and that also have a role in other aspects of RNA metabolism. These proteins might link nuclear events, such as RNA splicing, with the subsequent cytoplasmic localization of specific transcripts.

Active Transport, Cell Nucleus↗

PubMed1997

RNA transport in dendrites: a cis-acting targeting element is contained within neuronal BC1 RNA.

In nerve cells, a select group of RNAs has been localized to dendritic domains. Here we have examined dendritic RNA transport in sympathetic neurons in primary culture, using a microinjection protocol with neuronal BC1 RNA and with BC1-derived sequence segments. After cytoplasmic microinjection, full-length BC1 RNA was selectively transported to dendrites; in contrast, control RNAs such as nuclear RNAs and random-sequence irrelevant RNAs remained restricted to cytoplasmic areas proximal to the injection sites. Chimeric RNAs were constructed that contained the full-length BC1 sequence inserted upstream or downstream of the coding regions of nondendritic mRNAs. After microinjection, such chimeric RNAs were specifically targeted to dendrites; microinjected corresponding nonchimeric mRNAs were not. Dendritic transport of BC1 RNA was rapid: the average dendritic delivery rate within the first hour after microinjection was 242 +/- 25 microm/hr. Whereas a 5'-BC1 segment of 62 nucleotides was transported to dendrites to extents and at levels similar to full-length BC1 RNA, a 3'-BC1 segment of 60 nucleotides did not exit injected somata to any significant degree. A cis-acting dendritic targeting element is thus contained in the 5' part of neuronal BC1 RNA. These results demonstrate that mechanisms exist in neurons for fast and specific transport of selected RNAs to dendrites.

Animals↗

PubMed1983

Organ and species specificity of the messenger RNA transport factor.

The transport of messenger RNA from isolated rat liver nuclei is dependent on a 35,000 dalton protein localized in the cytoplasm. The tissue and species specificity of this protein are reported. The factor from female rat liver or from rat brain, kidney, or hepatoma supports the transport of messenger RNA from male rat liver nuclei. Messenger RNA is also transported in response to the factor from beef and chicken liver. The cytosols from rat erythrocytes, amoeba and yeast were inactive in the rat liver system. The results indicate that the messenger RNA transport factor is not specific for the nucleotide sequence of the coding portion of the messenger RNA and that it is not organ or species specific within the vertebrates.

Amoeba↗

PubMed1977

RNA transport in isolated myeloma nuclei. Transport from membrane-denuded nuclei.

Nuclei prepared from MOPC-21 cells were treated with the nonionic detergents Triton X-100 or Nonidet P-40. Chemical analysis revealed that nearly 90% of the nuclear phospholipid was removed by detergent treatment. The membrane-denuded nuclei remained intact with preservation of nuclear pore complexes as demonstrated by electron microscopy. Ribonucleic acid transport from detergent-treated nuclei proceeded at the same rate and to the same extent as in control nuclei. Normal nuclear restriction of nucleic acids was unaltered by removal of the nuclear membranes. The effect of temperature on transport of RNA from freshly isolated myeloma nuclei with intact nuclear envelopes was studied. No temperature transition was associated with the transport process. These data indicate that the transport of macromolecules from isolated myeloma nuclei is independent of the nuclear membrane.

Adenosine Triphosphate↗

PubMed2001

RNA commutes to work: regulation of plant gene expression by systemically transported RNA molecules.

Although long-distance movement of endogenous mRNAs in plants is well established, the functional contributions of these transported RNA molecules has remained unclear. In a recent report, Kim et al.2001 showed that systemically transported mRNA is capable of causing phenotypic change in developing tissue. Here, this finding and its significance are reviewed and discussed in detail. In addition, in order to give proper perspective, long-distance transport of other types of RNAs, e.g., RNA elicitors of post-transcriptional gene silencing and RNA genomes of plant viruses, and its possible regulation are discussed.

Biological Transport↗

PubMed1996

RNA transport to the vegetal cortex of Xenopus oocytes.

Xcat-2 RNA, a component of the germ plasm in Xenopus, localizes with the mitochondrial cloud material to the vegetal cortex in stage II oocytes. Vg1 RNA also localizes to the vegetal cortex, but later in stage III/IV oocytes, using a microtubule dependent pathway. To further analyze the mechanisms involved in RNA transport, in situ hybridization and autoradiography were used to follow the localization of endogenous Vg1 and injected Xcat-2 transcripts in stage IV oocytes. We show that Xcat-2 is competent to localize to the vegetal cortex quite independently of the mitochondrial cloud. Xcat-2 RNA appears to use the late Vg1 localization pathway, as depolymerization of microtubules by cold or nocodazole treatment prevented translocation of Xcat-2 transcripts, but did not result in the disruption of Xcat-2 anchored in the cortex. Furthermore, RNA transport was shown to be stage dependent for both Vg1 and Xcat-2 RNAs, as they did not localize in fully grown stage VI oocytes after injection. RNA sequences both required and sufficient to direct Xcat-2 to the vegetal cortex were mapped to a sequence of 150 nt immediately adjacent to the open reading frame and additional sequences at the end of the 3' untranslated region. Mapping was accomplished by injecting deletion mutant transcripts into stage IV oocytes and monitoring localization by RNase protection and autoradiography. All mutants competent for translocation were also capable of cortical anchoring, suggesting that the same signal is used for both steps. We speculate that two separate RNA pathways evolved during the course of Xenopus oogenesis. One pathway, specialized for the transport of germ plasm by way of the mitochondrial cloud, occurs early to ensure the segregation of the germ cell lineage. The other, late, pathway may serve as the more general transport system for localizing RNAs involved in somatic cell differentiation.

Animals↗

PubMed1990

Role of cytosol in the stimulation of RNA transport in vitro during cardiac hypertrophy in rats.

The 100,000 g supernatant isolated from hypertrophic hearts on fractionation by (NH4)2SO4 and DEAE-cellulose chromatography showed an enhanced RNA-transport activity when incubated with isolated nuclei from sham-operated hearts in vitro. Proteins of Mr 73,000, 68,000, 43,000 and 32,000 are enriched in the DEAE-cellulose fractions exhibiting maximal transport activity, and they are phosphorylatable. Pretreatment of the cytosol with antibodies to the Mr-68,000 and -32,000 proteins decreases the transport activity of the cytosol from 14% to 4.25%. Proteins of Mr 73,000, 68,000, 43,000 and 32,000 are translocated from the cytosol to the nuclear envelope under conditions of RNA transport in vitro. Our results here suggest that at least two of these proteins, those of Mr 68,000 and 32,000, play an indispensible role in the nucleocytoplasmic RNA transport in vitro. By making use of a specific myosin heavy-chain B-gene probe and hybridization, we have also shown the effect of cytosol on the transport of myosin heavy-chain mRNA from nucleus to cytosol.

Ammonium Sulfate↗

PubMed1989

[Age-related characteristics of RNA transport through the nuclear membrane].

The effect of cytosol and ATP-regenerating system on RNA, transport was studied in isolated liver nuclei of adult and old rats. The stimulating effect of cytosol was found not to depend on the age of animals. The release of RNA from old rat liver nuclei activated by the ATP-regenerating system was more expressed compared to adult rats. It is assumed that the age changes of energy-delivering system of the RNA transport through nuclear membrane may be conditioned by the deficit of endogenous energetic substrates in the hepatic cells of old animals.

Adenosine Triphosphate↗