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Results for “RNA Transport”

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At least 55 records · Page 3Linked to original sources
PubMed2003

RNA transport in oligodendrocytes from the taiep mutant rat.

The results presented here identify a new RNA trafficking phenotype in taiep oligodendrocytes that increases the frequency of reversals and restricts the extent of transport of RNA containing the A2RE transport signal from MBP mRNA. The taiep rat is a myelin mutant characterized by excessive accumulation of microtubules in oligodendrocytes and myelin deficiency in the central nervous system. The taiep RNA trafficking is developmentally correlated with the microtubule accumulation in oligodendrocytes and can be partially suppressed by reducing microtubule density with nocodazole or inhibiting dynein activity by coinjecting anti-dynein antibodies. These results suggest that RNA trafficking in taiep oligodendrocytes is inhibited by enhanced dynein activity that neutralizes or lessens the normal overriding power of the plus-end directed motor kinesin. Altered orientation of microtubules in oligodendrocyte fine processes and a physical barrier created by densely packed microtubules may also contribute to the inhibition of RNA trafficking in taiep oligodendrocytes.

Animals↗
PubMed1981

Some features of nucleo-cytoplasmic RNA transport from isolated nuclei.

Messenger RNA is released preferentially from isolated rat liver nuclei in the presence of the ATP-generating system and cytosol. The release is suppressed by spermidine, while cytoplasmic RNase inhibitor was ineffective and PCMB like some other thiol-blocking agents inhibitory. Cytoplasmic SOD added to the system strongly suppressed RNA release. A similar effect could be obtained by anaerobiosis due to addition of SMP. In both cases the inhibition is reversed by cyanide. In contrast to normal liver where the generation of superoxide radicals takes place almost exclusively in microsomes and is coupled with the oxidation of NADPH, in mouse ascites hepatoma 22a the generation of superoxide radicals occurs mainly in the nuclear envelope and is coupled wih the oxidation of both NADPH and NADH and inhibited by cyanide.

Animals↗
PubMed1984

Modulation of RNA transport by polyvinylpyrrolidone.

A number of studies have documented substantial loss of nuclear protein during aqueous nuclear isolation procedures. This loss can, to some extent, be counteracted by addition of impermeable macromolecules like polyvinylpyrrolidone, which prevent nuclear swelling. While nucleic acids appear to be much less susceptible to leakage during isolation, the effects of these additives on RNA release during in vitro incubation have not been examined. Here we show that addition of polyvinylpyrrolidone results in significant decreases in RNA transport; inhibition becomes maximal at 50-75 microM addition.

Animals↗
PubMed1992

Evidence for a highly selective RNA transport system and its role in establishing the dorsoventral axis of the Drosophila egg.

The specification of cell fates along the dorsoventral axis of the Drosophila embryo is dependent on the asymmetric distribution of proteins within the egg and within the egg's outer membranes. Such asymmetries arise during oogenesis and are dependent on multiple cell-cell interactions between the developing oocyte and its neighboring somatic follicle cells. The earliest known such interaction involves the generation of a signal in the oocyte and its reception in the follicle cells lying on the dorsal surface of the oocyte at approximately stage 10 of oogenesis. Several independent lines of investigation indicate that the fs(1)K10 (K10) gene negatively regulates the synthesis of the signal in the oocyte nucleus. Here we present data that indicate that the accumulation of K10 protein in the oocyte nucleus is a multistep process involving: (1) the synthesis of K10 RNA in nurse cells, (2) the rapid transport of K10 RNA from nurse cells into the oocyte, (3) the localization of K10 RNA to the anterior margin of the oocyte, and (4) K10 protein synthesis and localization. K10 RNA is transported into the oocyte continuously beginning at approximately stage 2. This indicates a high degree of selectivity in transport, since most RNAs synthesized in stage 2 and older nurse cells are stored there until stage 11, when nurse cells donate their entire cytoplasm to the oocyte. The sequences responsible for the early (pre-stage 11) and selective transport of K10 RNA into the oocyte map to the 3' transcribed non-translated region of the gene. None of the other identified genes involved in dorsoventral axis formation are required for K10 RNA transport.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed2003

Dual regulated RNA transport pathways to the cortical region in developing rice endosperm.

Prolamine and glutelin RNAs are localized to two subdomains of the cortical endoplasmic reticulum (ER), the protein body ER and the cisternal ER, in developing rice seeds. The addition of nearly full-length prolamine sequences at the 3' untranslated region of a reporter RNA redirects its localization from the cisternal ER to the protein body ER. Deletion analysis of prolamine RNA sequences indicates the presence of two partially redundant cis elements required for protein body ER targeting. The addition of glutelin 3' untranslated region to protein body ER cis sequences, however, redirects RNA localization to the cisternal ER. These results indicate that there are at least two regulated RNA transport pathways as well as a constitutive pathway to the cortical ER.

3' Untranslated Regions↗
PubMed1991

Expression of mouse serotonin transporter RNA in Xenopus laevis oocytes.

The serotonin transporter removes serotonin from the synapse, terminating the action of this neurotransmitter. We have taken an initial step towards cloning the serotonin transporter by obtaining its expression in Xenopus oocytes. We found that mouse brainstem is a suitable source of serotonin transporter mRNA and that synthesis of the transporter in injected oocytes occurs steadily over a 3 day period. Uptake of [3H] serotonin was inhibited by 18 nM citalopram, a specific inhibitor of serotonin transport.

Animals↗
PubMed2001

Conserved signals and machinery for RNA transport in Drosophila oogenesis and embryogenesis.

Localization of cytoplasmic messenger RNA transcripts is widely used to target proteins within cells. For many transcripts, localization depends on cis-acting elements within the transcripts and on microtubule-based motors; however, little is known about other components of the transport machinery or how these components recognize specific RNA cargoes. Here, we show that in Drosophila the same machinery and RNA signals drive specific accumulation of maternal RNAs in the early oocyte and apical transcript localization in blastoderm embryos. We demonstrate in vivo that Egalitarian (Egl) and Bicaudal D (BicD), maternal proteins required for oocyte determination, are selectively recruited by, and co-transported with, localizing transcripts in blastoderm embryos, and that interfering with the activities of Egl and BicD blocks apical localization. We propose that Egl and BicD are core components of a selective dynein motor complex that drives transcript localization in a variety of tissues.

Animals↗
PubMed2002

The spread of tobacco mosaic virus infection: insights into the cellular mechanism of RNA transport.

Interactions of plant cells with pathogens or other biotic or abiotic environmental factors can give rise to systemic defense responses that rely upon the cell-to-cell and systemic transport of specific signals. A novel type of systemic signaling was revealed by recent evidence indicating the existence of RNA species that travel cell to cell and through the vasculature. The most compelling evidence for intercellular and systemic transport of RNA in plants is provided by viroids and viruses that apparently use the endogenous transport machinery to spread infection. The cell to cell movement of plant viruses occurs through small pores in the cell wall known as plasmodesmata and depends on virus-encoded 'movement proteins'. This review summarizes current knowledge of Tobacco mosaic virus infection with emphasis on the mechanism by which this virus targets its RNA genome from sites of replication to plasmodesmata to achieve intercellular spread.

Actin Cytoskeleton↗
PubMed1987

Vesicular stomatitis virus in Drosophila melanogaster cells: lack of leader RNA transport into the nuclei and frequent abortion of the replication step.

In cultured Drosophila melanogaster cells, vesicular stomatitis virus (VSV) establishes a persistent, noncytopathic infection. No inhibition of host macromolecular synthesis occurs. We studied the synthesis of VSV plus-strand leader RNA, which may be directly involved in vertebrate host synthesis shut-off. Leader RNA accumulated in Drosophila cell cytoplasm, but in low amounts, it was either free or associated to structures larger than the leader RNA-N protein complexes found in vertebrate cells. Only a few leader RNA copies migrated into the cell nucleus; no increase of this transport was observed at any time during the virus cycle. Viral RNAs complementary to the 3' end of the genome and ranging in size from the leader to several hundred nucleotides were found to accumulate in Drosophila cell cytoplasm. Their synthesis was inhibited in the presence of cycloheximide, which blocks all protein synthesis and VSV replication. Correlation between the absence of VSV cytopathogenicity in Drosophila cells and the lack of leader RNA transport into their nuclei is discussed, as well as the possible relationship between the restriction of viral synthesis and the frequent initiation of an abortive replication step.

Animals↗
PubMed1983

Effect of cytosol on transport of RNA in vitro during cardiac hypertrophy.

An enhanced RNA-transport activity was observed in vitro from nuclei obtained from animals with cardiac hypertrophy as compared with that of sham-operated controls. The 100 000 g supernatants obtained from hypertrophic hearts stimulated the RNA transport from nuclei of sham-operated controls, and this stimulation was maximum with 40% supernatant. Ca2+- and nucleic acid-dependent ATPase and alkaline phosphatase activities, which may be involved in an energy-dependent transport, were high in nuclei from hypertrophic hearts, and the nuclei of sham-operated animals showed higher activities of these enzymes after incubation with supernatant from hypertrophic hearts, which stimulates the RNA transport in vitro from nuclei of sham-operated animals.

Adenosine Triphosphatases↗
PubMed1994

A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA transport and nuclear pore distribution.

Temperature-sensitive nucleoporin nup49-316 mutant cells accumulate poly(A)+ RNA inside the nucleus when shifted to restrictive temperature. We performed a synthetic lethal screen with this mutant allele to identify further components of the mRNA export machinery. A synthetic lethal mutant slv21 was isolated, which exhibited a ts phenotype and showed nuclear accumulation of poly(A)+ RNA at 37 degrees C. The wild-type gene complementing slv21 was cloned and sequenced. It encodes a novel protein Nup133p which is located at the nuclear pore complex. NUP133 is not an essential gene, but cells in which NUP133 is disrupted grow slowly at permissive temperatures and stop growing at 37 degrees C. Concomitant with the growth inhibition, nup133- cells accumulate poly(A)+ RNA inside the nucleus whereas nuclear import of a karyophilic reporter protein is not altered. Strikingly, nup133- cells display extensive clustering of nuclear pore complexes at a few sites on the nuclear envelope. However, the nuclear pore clustering phenotype and intranuclear accumulation of poly(A)+ RNA are not obligatorily linked, since an amino-terminally truncated Nup133p allows normal poly(A)+ RNA export, but does not complement the clustering phenotype of nup133- cells.

Amino Acid Sequence↗
PubMed1983

Characterization of a messenger RNA transport protein.

A cytoplasmic protein which facilitates the energy-dependent transport of mRNA from isolated nuclei to a specified medium has been further characterized, since it could have relevance to the mechanism of mRNA nucleo-cytoplasmic transport in vivo. This protein is now shown, by cDNA hybridization analysis using appropriate recombinant probes, to be obligatory for the transport of alpha 2u-globulin and albumin mRNA from male rat liver nuclei. It is concentrated in the cytoplasm. When isolated under conditions where they retain nuclear proteins, the nuclei contain less than 2% of the total mRNA transport activity. Approx. 20% is recovered in the cytosol, while the rest (80%) copurifies with the messenger ribonucleoproteins in the polyribosome fraction. The protein is eluted from the poly A-messenger ribonucleoproteins between 0.25 and 0.50 M NaCl. The activities of the cytosolic- and messenger ribonucleoprotein-derived transport proteins were mutually additive below saturation of the transport system. Further, the activities of both fractions were increased when they were fortified with the catalytic subunit of the cAMP-dependent protein kinase in the presence of ATP. On the other hand, protein kinase-induced thiophosphorylation of the protein with ATP[S] decreased transport activity. The molecular weight of the transport protein from either cell compartment as judged by molecular sieving is approx. 35,000. It has now been purified 2000-fold and requires manganese ions and serum albumin for stabilization of activity. The highly purified transport factor from the cytosol is tentatively assigned a molecular weight of 32,000 by SDS-polyacrylamide gel electrophoresis.

Alpha-Globulins↗
PubMed1966

RNA transport from nucleus to cytoplasm in Chironomus salivary glands.

The fine structure and cytochemistry of the extremely large RNA puffs, or Balbiani rings, in salivary gland nuclei of midge, Chironomus thummi, larvae have been investigated. The Balbiani rings are composed of a diffuse mass of electron-opaque 400 to 500 A granules, short threads about 180 to 220 A in diameter and associated fine chromatin fibrils. These components appear to be organized into brushlike elements which form the ring. Electron microscope cytochemistry has shown that the granules and short threads contain RNA. After ribonuclease digestion, only 50 to 100 A chromatin fibrils were apparent in the Balbiani ring, and the granules were no longer demonstrable. Deoxyribonuclease digestion had no apparent effect on these structures. Observations indicate that the granules are formed from the short threads and released into the nucleoplasm in which they are evenly distributed. At the nuclear envelope, many granules have been observed partially or completely within the nuclear pores. These granules become elongated and are shown to penetrate the center of the pore in a rodlike form, about 200 A in diameter. The Balbiani ring granules are not normally visible within the cytoplasm adjacent to the nuclear envelope, but have been rarely found in this region. It is suggested that the granules represent the product of the Balbiani ring, possibly a messenger RNA bound to protein, and that they regularly pass into the cytoplasm through a narrow central channel in the pores of the nuclear envelope.

Animals↗
PubMed2000

Multiple copies of the Mason-Pfizer monkey virus constitutive RNA transport element lead to enhanced HIV-1 Gag expression in a context-dependent manner.

Retroviral gene expression requires nuclear export and translation of incompletely spliced RNA. In the case of human immunodeficiency virus (HIV), this is facilitated by the viral Rev protein binding to its cognate RNA response element (RRE), while other retroviruses contain constitutive transport elements (CTE) binding to cellular factors. These CTE can substitute for the HIV-1 Rev/RRE system, albeit with reduced efficiency. Here, we show that multimeric copies of the CTE restore HIV-1 protein expression to levels comparable to or higher than Rev/RRE in various cell lines from different species. We suggest that multimerization of export factors is important for CTE function, as reported for Rev. CTE function was not affected when the element was displaced from its natural position close to the poly(A) signal, while insertion of an intron into the 3'-untranslated region (3'-UTR) severely reduced CTE activity. In this case, cytoplasmic RNA degradation was observed, which may be mediated by nonsense-mediated RNA decay. In contrast, Rev-dependent gene expression was insensitive to an intron in the 3'-UTR. Finally, we show that the putative CTE-binding protein RNA helicase A is not specifically translocated into the cytoplasm upon overexpression of CTE-containing RNA.

3' Untranslated Regions↗