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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ribonucleoprotein particles present in extracts of nuclei prepared from Tetrahymena pyriformis labelled for 1, 2.5, 5 and 10 min with [3H]uridine during exponential growth were analysed by sedimentation through linear 10--30% sucrose gradients. After 1 min of labelling, the early ribosomal RNA precursor (36-S) is found to be associated with slowly sedimenting particles which form a broad peak centred at approximately 50 S. Other kinds of particles sedimenting at 80 S, 66 S, 60 S and 44 S are observed when labelling is carried out for longer periods (2.5, 5 and 10 min). The 80-S particle contains 29-S and 18-S RNA species together with traces of 36-S RNA; the 60-S and 44-S particles contain 26-S and 17-S RNAs respectively. Similar results were obtained when [Me-3H]methionine was used for labelling in place of [3H]uridine. Methylation of the RNA present in slowly sedimenting nuclear components (30-70-S) is rapid, reaching a plateau at 5 min while that of the faster sedimenting (70--90-S) components is still increasing after 10 min. Only three types of ribonucleoprotein particles (80-S, 66-S, and 44-S) were observed when the cells were labelled after prolonged starvation. A scheme of ribosome biogenesis based on these results is presented.
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PMID:Characterization of preribosomal ribonucleoprotein particles from Tetrahymena pyriformis. 11 76

Mouse sarcoma ascites cells do not utilize fully their capacity for protein synthesis. A considerable portion of their ribosomes occur as inactive monomers. Also, a substantial amount of the cellular mRNA is in the form of ribonucleoprotein particles that sediment in the 20-70S range. This is indicated both by measurements of poly(A) content and by translation of the RNA in cell-free systems. The population of polypeptides synthesized under the direction of the RNA from these particles is less heterogeneous than that directed by RNA from polysomes. The mRNAs for some polypeptides are present predominantly in the small particles. Others are distributed to varying degrees between particles and polysomes. Incubation of the cells with cycloheximide drives most of the ribosomal monomers and a portion of the untranslated mRNA into polysomes. Some of the mRNAs that were predominantly in the inactive fraction seem to be refractory to this treatment. Particles released from polysomes in cells subjected to starvation are quite effective in promoting polypeptide synthesis in a reticulocyte cell-free system and cause the synthesis of a population of polypeptides similar to that coded by the polysomal RNA. The particles from cells exposed to cycloheximide are inactive but yield active RNA upon deproteinization. It is suggested that some mRNA species are maintained in an inactive state in the cell by a component of the nucleoprotein complex.
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PMID:Inactive mRNA-protein complexes from mouse sarcoma-180 ascites cells. 29 64

The round nucleoli of chick embryo myoblasts, when grown in a culture medium devoid of arginine, unravel in several days into 5-20 micro long, beaded strands termed nucleolar necklaces (NN). Addition of arginine reverses this change. The NN contain protein, RNA, and traces of DNA as determined cytochemically by enzyme digestion and by acridine-orange fluorescent staining. When a cell containing the beaded strand is treated with agents, such as actinomycin D, that prevent rRNA polymerase action, the strand collapses and condenses into a small dense nucleolus with segregated regions of ribonucleoprotein (RNP) and deoxyribonucleoprotein (DNP). The properties of the NN appear to resemble those of the nucleolar necklaces of amphibian oocytes. Cycloheximide or puromycin inhibition of general protein synthesis does not lead to NN formation. We suggest that NN formation during arginine starvation may be a result of a singular depletion of some rapidly turning over, arginine-rich proteins that normally attach to ribosomal RNA precursor molecules during their synthesis in the processing towards maturation of the ribosomes.
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PMID:Nucleolar necklaces in chick embryo myoblasts formed by lack of arginine. 410 77

Starvation induces vegetative microplasmodia of Physarum polycephalum to differentiate into translationally-dormant sclerotia. The existence and the biochemical nature of stored mRNA in sclerotia is examined in this report. The sclerotia contain about 50% of the poly (A)-containing RNA [poly(A)+RNA] complement of microplasmodia as determined by [3H]-poly(U) hybridization. The sclerotial poly(A)+RNA sequences are associated with proteins in a ribonucleoprotein complex [poly(A)+mRNP] which sediments more slowly than the polysomes. Sclerotial poly(A)+RNP sediments more rapidly than poly(A)+RNP derived from the polysomes of microplasmodia despite the occurrence of poly(A)+RNA molecules of a similar size in both particles suggesting the existence of differences in protein composition. Isolation of poly(A)+RNP by oligo (dT)-cellulose chromatography and the analysis of its associated proteins by polyacrylamide gel electrophoresis show that sclerotial poly(A)+RNP contains at least 14 major polypeptides, 11 of which are different in electrophoretic mobility from the polypeptides found in polysomal poly(A)+RNP. Three of the sclerotial poly(A)+RNP polypeptides are associated with the poly(A) sequence (18, 46, and 52 x 10(3) mol. wt. components), while the remaining eight are presumably bound to non-poly(A) portions of the poly(A)+RNA. Although distinct from polysomal poly(A)+RNP, the sclerotial poly(A)+RNP is similar in sedimentation behavior and protein composition (with two exceptions) to the microplasmodial free cytoplasmic poly(A)+RNP. The results suggest that dormant sclerotia store mRNA sequences in association with a distinct set of proteins and that these proteins are similar to those associated with the free cytoplasmic poly(A)+RNP of vegetative plasmodia.
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PMID:Stored messenger ribonucleoprotein particles in differentiated sclerotia of Physarum polycephalum. 617 47

Four major mRNA species of mouse sarcoma ascites cells, coding for polypeptides designated P65, P40, P36, and P21, occur predominantly as untranslated messenger ribonucleoprotein particles. Cloned cDNA probes were used to study their distribution in cytoplasmic extracts of these cells. A considerable portion of the mRNA molecules sedimented as small particles, whereas the rest was present in polyribosomes. In contrast, the actin mRNA was present almost exclusively in polyribosomes. Incubation of the ascites cells in culture medium, particularly after a starvation treatment, caused an enhancement in polypeptide chain initiation relative to elongation in these cells, as evidenced by a shift of ribosomes into the polyribosome fraction and by an increase in polyribosome size. Exposure of the cells to a low concentration of cycloheximide, an inhibitor of the elongation step, had a similar effect. The actin mRNA and the active P65, P40, P36, and P21 mRNA molecules were shifted to larger polyribosomes in the treated cells, but no shift of molecules from small particles to polyribosomes was observed. The incubation in culture also led to considerable increases in the proportion of P65 and P40 mRNA molecules in the untranslated state. The results indicate that the untranslated state cannot be attributed to poor initiation efficiency. It is suggested that a portion of the mRNA molecules is maintained in a repressed state and that mRNA repression may represent an important translation control process.
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PMID:Messenger RNA species partially in a repressed state in mouse sarcoma ascites cells. 696 92

Most Saccharomyces cerevisiae strains carry in their cytoplasm 20 S RNA, a linear single-stranded RNA molecule of 2.5 kilobases in size. 20 S RNA copy number is greatly induced in stress conditions such as starvation, with up to 100,000 copies per cell. 20 S RNA has coding capacity for a protein of 91 kDa (p91) with sequences diagnostic of RNA-dependent RNA polymerases of (+) strand and double-stranded RNA viruses. We detected p91 in 20 S RNA-carrying strains with specific antisera. The amount of p91 in growing cells is higher than that of stationary cells and similar to the one in 20 S RNA-induced cells. Although 20 S RNA is not encapsidated into viral particles, p91 non-covalently forms a ribonucleoprotein complex with 20 S RNA. This suggests a role of p91 in the RNA to RNA synthesis processes required for 20 S RNA replication. Although the strain analyzed also harbors 23 S RNA, a closely related single-stranded RNA, 23 S RNA is not associated with p91 but with its putative RNA polymerase, p104. Similarly, 20 S RNA is not associated with p104 but with p91. These results suggest that 20 S RNA and 23 S RNA replicate independently using their respective cognate RNA polymerases.
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PMID:Yeast viral 20 S RNA is associated with its cognate RNA-dependent RNA polymerase. 765 26

The fragile X syndrome results from a transcriptional silencing of the FMR1 gene and the absence of its encoded protein. FMRP is a cytoplasmic RNA-binding protein, whose specific cellular function is still unknown. We present evidence that virtually all detectable cytoplasmic FMRP in mouse NIH 3T3 and human HeLa cells is found strictly in association with mRNA in actively translating polyribosomes. Furthermore, FMRP released from polyribosomes is associated with ribonucleoprotein complexes with sedimentation coefficients of 60-70S and selection on oligo(dT)-cellulose reveals that this association is specific to poly(A)-containing mRNPs. This association with actively translating polyribosomes is not affected by alteration of translational processes induced by serum stimulation and starvation in NIH 3T3 cells, suggesting that FMR1 expression is not cell cycle regulated and that FMRP might have a house-keeping function. FXR2 protein, which is closely related to FMRP, is also detected associated with mRNPs in translating polyribosomes. The results strongly suggest that FMRP might be a mRNA chaperone interacting with mRNP complexes.
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PMID:The fragile X mental retardation protein is associated with poly(A)+ mRNA in actively translating polyribosomes. 928 83

Previous experiments have revealed a relatively weak electrostatic binding capacity of in vitro reconstituted intermediate filaments (IFs) as well as of natural IFs of whole cell mount preparations for purified ribosomal particles of mammalian origin. In order to demonstrate that such associations also occur in vivo, intact cells were subjected to double immunofluorescence microscopy using antibodies directed against vimentin and ribosomal protein S17. Since in proliferating cells the majority of the ribosomal particles are assembled into polyribosomes and these are to a great extent associated with microfilaments, in vitro cultured mouse embryo skin fibroblasts (MSF cells) were treated with puromycin to allow the formation of single ribosomes. Employing confocal laser scanning microscopy, the ribosomes were detected in colocalization with vimentin IFs. Disassembly of polyribosomes was also achieved by serum starvation of cultured cells. In this case, MSF cells of a low passage attained an extended and flattened appearance with the vimentin IFs being directly associated with the cell nuclei, radiating into the peripheral areas of the cells or showing a stress fiber-like distribution. In both cases, considerable quantities of ribosomal material were seen in close neighborhood to vimentin IFs. Frequently, these ribosome-IF associations were coaligned with microtubules and they also surrounded myosin I-decorated stress fibers. Double labeling with the vital, RNA-specific fluorochrome SYTO 14 produced a fluorescence pattern largely superimposable on that of ribosomal protein S17. Treatment of the starved cells with either demecolcine or cytochalasin D had an only moderately disturbing effect on vimentin IF distribution and the ribosomes stayed in contact with the vimentin IFs. On the basis of these results, it is conceivable that IFs play a role in the storage of ribonucleoprotein particles in general and non-translating ribosomes in particular in the cytoplasm of animal cells. In addition, the often seen coalignment of IFs with microtubules and microfilaments might serve facilitated and directional transport of ribonucleoprotein particles from the nucleus to peripheral areas of the cell.
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PMID:Colocalization of single ribosomes with intermediate filaments in puromycin-treated and serum-starved mouse embryo fibroblasts. 980 Mar 50

Rat liver was homogenized in 0.88 M sucrose. The DNA and total RNA were determined, and the homogenate was fractionated by differential centrifugation. The pellets obtained between 30 minutes at 20,000 g and 180 minutes at 105,000 g were analyzed for RNA and nitrogen. The ribonucleoproteins were determined in the analytical ultracentrifuge. The non-pellet RNA was calculated by difference. The results are reported as amounts per 6.7 x 10(-9) mg. of DNA. In young, growing male rats the amounts of microsomal protein and ribonucleoprotein B (83S) increased with age. Non-pregnant adult females showed less non-pellet RNA and much more ribonucleoprotein C (63S) than did adult males. During pregnancy both of these cell constituents reverted to levels characteristic for male animals. Starvation for 5 days resulted in a reduction in the mass of liver tissue, the non-pellet RNA, the microsomal protein, and ribonucleoproteins B and C. During recovery from starvation the return of the liver to normal paralleled the rate at which body weight was restored. Treatment with cortisone, 25 mg. per rat per day for 5 days, caused an increase in microsomal protein and a decrease in ribonucleoprotein B. Treatment with 6-mercapto-purine, 50 mg. per kilo per day for 5 days, caused little change in liver composition in either males or females.
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PMID:The influence of age, sex, pregnancy, starvation, and other factors on the cytoplasmic ribonucleoproteins of rat liver. 1361 Sep 43

Sypherd, Paul S. (University of California, San Diego). Accumulation of ribonucleoprotein particles in a relaxed mutant of Escherichia coli. J. Bacteriol. 90:403-410. 1965.-The synthesis of ribonucleic acid during amino acid deprivation of a "relaxed" mutant was investigated. Aspects of the stability of the macromolecular ribonucleic acid (RNA) were studied, and standard conditions were established to allow maximal recovery of the larger RNA's (i.e., 16S and 23S). These RNA's, representing 75% of the total RNA produced during starvation, were present in particles with nominal S-values of 20, 30, and 43. The particles are extremely sensitive to nuclease action, being completely destroyed in the presence of 2 mug/ml of pancreatic ribonuclease at 15 C for 30 min. The particles containing the bulk of the RNA were shown to be ribonucleoprotein, consisting of 26 to 28% protein by weight. It was shown that no mature 70S ribosomes were formed during the accumulation of the lighter, protein-deficient particles.
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PMID:ACCUMULATION OF RIBONUCLEOPROTEIN PARTICLES IN A RELAXED MUTANT OF ESCHERICHIA COLI. 1432 53


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