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PubMedDate not supplied

[The role for nucleus-associated polyribosomes in the coordination of histone synthesis with replication of chromosomal DNA in loach embryonic cells].

During intensive chromosome replication in loach (Misgurnus fossilis) embryonic cells a particular class of nucleus-associated polyribosomes has been discovered alongside the free and membranebound polyribosomes. The comparison of the translational patterns of these three polyribosome classes in in vivo and in vitro conditions has proved their metabolic and functional difference. It has been shown that the nucleus-associated polyribosomes comprising over 50 per cent of all the cell polyribosomes in the above-mentioned period produce the bulk of lysine-rich histones on the newly formed mRNAs. Using metabolic inhibitors of DNA, or RNA, or protein synthesis it has been established that the nucleus-associated polyribosome functional activity as differs from that of free and membrane-bound polyribosomes and depends to great degree on the chromosomal DNA replication and the shortliving mRNAs transcription. The data obtained suggest that the chromatin biogenesis control can be achieved by spacial coupling between DNA replication and histone synthesis at the nuclear envelope level.

Animals↗
PubMedDate not supplied

[Intracellular localization of fibronectin-synthesizing polyribosomes using I125 collagen].

Interaction of 125I-collagen with fibronectin-synthesizing polyribosomes, isolated from 9 days old chicken embryos, was studied. The interaction was maximal at the ratio of 0.1 microgram 125I-collagen and 5 ou of polyribosomes. Specific reaction of 125I-collagen with fibronectin polypeptides growing on polyribosomes was estimated by means of antibodies to fibronectin inhibiting the complex formation of polyribosomes-125I-collagen. The antibodies were shown to decrease the reaction rate of total polyribosomes (free and membrane-bound) with 125I-collagen by 25.4% and of free polyribosomes - by 6.7%. The data obtained suggest that fibronectin is synthesized mainly on polyribosomes, bound with the membranes of endoplasmic reticulum.

Animals↗
PubMed1981

[Properties of rat liver polyribosomes synthesizing transferrin].

A radioimmunological study of rat liver polyribosomes synthesizing transferrin was carried out. The 125I-labelled monospecific antibodies against transferrin interact with membrane-bound liver polyribosomes to form a specific antigen-antibody complex. No binding of 125I-antibodies against transferrin to free liver polyribosomes was observed. The transferrin polyribosomes contain 11-13 monoribosomes per 1 molecule of mRNA. An injection of cycloheximide to the animals results in an increase in the size of the transferrin polyribosomes up to 16 monoribosomes per 1 mRNA molecule. During translation of the liver polyribosomal fractions in a cell-free system of wheat embryos only the membrane-bound polyribosomes were capable to synthesize immunoprecipitated transferrin.

Animals↗
PubMed1979

Isolation of ribonuclease-free intact polyribosomes from rat kidney.

High levels of RNAase present in rat kidney have prevented isolation of intact polyribosomes from this tissue. This problem has been circumvented by a thorough in situ arterial perfusion of rat kidney, coupled with homogenization of the perfused rat kidney in heparin and detergents-fortified high-speed supernatant prepared from rat liver. This procedure reduced RNAase activity in the homogenate by as much as 70%. Sedimentation of the polyribosomes from this homogenate through a layer of 2.0 M sucrose resulted in a 78--80% yield of polyribosomes from the rat kidney. The resulting polyribosomal pellet contained less than 8% of the RNAase activity present in polyribosomes from non-perfused rat kidney. The remaining RNAase activity was separated from the larger polyribomes by sucrose density gradient centrifugation. The majority of the polyribosomes were larger than tetramers. This procedure also incrased both the yield and size of polyribosomes from rat and mouse liver.

Animals↗
PubMed1966

Polyribosomes in rat-liver preparations.

1. The distribution of rat-liver polyribosomes in sucrose density gradients has been investigated with regard to the effects of the preparative procedures and the physiological and pathological condition of the animal. 2. By using carefully defined conditions, three principal polyribosomal fractions have been isolated with S(20,w) values of 340, 275 and 225s in addition to the dimerized 120s and single 80s ribosomes. 3. The polyribosomes were very sensitive to treatment with ribonuclease and to mechanical stresses. 4. Incubation of dispersed hepatic cells and also cell-free preparations with puromycin in the presence of ATP and phosphoenolpyruvate caused rapid partial degradation of the polyribosomes. Treatment of the dispersed cells with actinomycin D also degraded the polyribosomes. 5. The liver polyribosomes of rats not raised under pathogen-free conditions and possibly of rats with an arthritic syndrome may be more fragile than those of healthy pathogen-free animals. 6. Treatment of pathogen-free rats with drugs stimulating liver anabolism profoundly affected the distribution of polyribosomes in sucrose density gradients.

Animals↗
PubMed1971

Biosynthesis in vitro of tryptophanase by polyribosomes from induced cultures of Escherichia coli.

1. Polyribosomes were isolated from Escherichia coli grown in media in which tryptophanase is induced and in which it is repressed. The polyribosomes from the induced bacteria had a small amount of tryptophanase activity associated with them. 2. A portion of the enzyme activity remained bound to polyribosomes during centrifuging in sucrose gradients. 3. Incubation of tryptophanase-containing polyribosomes with puromycin released enzyme activity. 4. The binding of the enzyme to the polyribosomes did not depend on the presence of DNA. 5. When the polyribosomes were incubated under conditions of protein synthesis with supernatant fraction obtained from repressed bacteria, a small but statistically significant increase in enzyme activity was produced. 6. When a radioactive amino acid was included in the incubation mixture for the tryptophanase system a radioactive protein was obtained whose chromatographic, electrophoretic and sedimentation properties were identical with those of tryptophanase. 7. The amount of incorporation was consistent with the amount of new enzyme synthesis predicted by the increase in enzyme activity. Both radioactive incorporation and increase in enzyme activity were shown to be energy-dependent and also negative controls were obtained by using zero-time incubations or polyribosomes isolated from either repressed cells or a mutant lacking the ability to produce tryptophanase. 8. The distribution of radioactive leucine in the carboxyl region of the newly labelled tryptophanase was examined by digesting the labelled protein with carboxypeptidases. It was shown that the radioactivity was more highly concentrated towards the carboxyl terminus when the incubation times for protein synthesis were shorter (implying that, with longer incubation times, longer lengths of polypeptide chain contained radioactive amino acid residues).

Bacterial Proteins↗
PubMed1967

Occurrence, isolation, and characterization of polyribosomes in yeast.

This report details the procedural requirements for preparing cell-free extracts of yeast rich in polyribosomes. This enabled us to demonstrate the occurrence of polyribosomes in yeast, to show their role in protein synthesis, and to devise methods for their resolution and isolation. When certain precautions are met (the use of log phase cells, rapidly halting cell growth, gentle methods of disruption, sedimentation through exponential density gradients, etc.), individual polyribosome size classes ranging up to the heptosome can be fractionated and separated from their nearest neighbors. Larger size classes are resolved partially among themselves, free of smaller polyribosomes. This was confirmed by extensive electron micrographic studies of material from the various fractions obtained upon density gradient centrifugation of yeast extracts. Modifications of the gradients and procedure should allow fractionation and isolation of the larger polyribosomes, including those containing polycistronic messages. Yeast polyribosomes are disaggregated to single ribosomes by longer term grinding, cell disruption by the French pressure cell, the Hughes press, or by incubation with dilute RNAse. Yeast polyribosomes are active in the incorporation of amino acids into polypeptide; the single ribosomes exhibit only slight activity. The latter activity is probably due to the presence of a small fraction of monosomes still containing mRNA. Poly-U stimulates amino acid incorporation only in the single ribosomes.

Cell Division↗
PubMed1970

Drosophila polyribosomes. The characterization of two populations by cell fractionation and isotopic labeling with nucleic acid and protein precursors.

Two populations of polyribosomes have been isolated from third instar larvae of D. melanogaster. One population appeared to be soluble while the second seemed membrane-bound. Short-term labeling of the two RNP fractions with radioactive nucleic acid and protein precursors was achieved by using a feeding stimulant. RNA was extracted from both polyribosomal fractions following 25, 40, and 60 min of in vivo uridine-(3)H incorporation. Soluble polyribosomes exhibited more rapid uptake of uridine into ribosomal and heterogeneous RNA fractions than did membrane-bound polyribosomes at comparable time periods. In vivo amino acid incorporation into the two polyribosomal populations was examined after 10, 20, 40, 60, and 80 min of incubation in leucine-(3)H. In this case, the membrane-bound polyribosomes reached a higher specific activity than did the soluble ones. These functional differences confirmed the observation, based on cellular fractionation studies, that the two classes of polyribosomes represented functionally distinct populations. These data have been compared with those from studies on other metazoan systems. In addition, dithiothreitol has been demonstrated to be a powerful ribonuclease inhibitor.

Amino Acids↗
PubMed1970

Rapid Changes in Levels of Polyribosomes in Zea mays in Response to Water Stress.

Sucrose gradient profiles of polyribosomes from the coleoptilar node region of seedlings of Zea mays L. were obtained without pelleting and redispersion of the particles. Water stress caused a shift of ribosomes from the polymeric to the monomeric form, starting about 30 minutes after stress initiation and when the water potential of the tissue began to decrease measurably. After about 4 hours of stress (a decrease in tissue water potential of about 5 bars), most of the higher polymers of ribosomes had shifted to monoribosomes. Release of stress caused the ribosomes to revert from monomeric to polymeric form after a lag period apparently determined by the extent of prior stress. Use of bentonite and isolation of polyribosomes from combined stressed and control tissue gave results indicating that the reduced polyribosomal level was not an artifact caused by ribonuclease during isolation.Incubating roots in cycloheximide (2 micrograms per milliliter) had no effect on the proportion of polyribosomes in control roots, but it prevented the loss of polyribosomes caused by stress. Since cycloheximide inhibits the release of nascent polypeptide from polyribosomes, it appears possible that stress-effected loss in polyribosomes occurs only if polypeptides can be terminated and released.

Journal Article↗
PubMed1979

Stability of messenger ribonucleic acid of free and membrane-bound polyribosomes of the livers of rats treated with ethionine.

Administration of ethionine to female rats results in disaggregation of free and membrane-bound polyribosomes and inhibition of protein synthesis in the liver. The administration of adenine and methionine to ethionine-treated rats reverses these effects, even after actinomycin D treatment which inhibits new RNA synthesis. The membrane-bound polyribosomes show greater recovery of the state of aggregation and of in vitro protein synthesis than do the free polyribosomes of rat liver. The messenger RNA (mRNA) in the recovering membrane-bound polyribosomes appears to come from endoplasmic reticulum membranes and is not related to increased nucleocytoplasmic translocation of existing mRNA. Initiation factors-dependent stimulation of polyphenylalanine synthesis by ribosomes and by initiation factors of membrane-bound polyribosomes is increased more than the synthesis by ribosomes and by initiation factors of free polyribosomes in the livers of ethionine-treated rats receiving actinomycin D and adenine plus methionine. Our results suggest that stable mRNA associated with membranes remains in the rat liver after injury by ethionine, and during recovery induced by adenine and methionine, the mRNA is utilized to reform membrane-bound polyribosomes.

Adenine↗
PubMed1992

Differential effects of iron and inflammation on ferritin synthesis on free and membrane-bound polyribosomes of rat liver.

We have examined the distribution of ferritin mRNA to free and endoplasmic reticulum (ER)-bound liver polyribosomes during inflammation and iron treatment of rats. Postnuclear tissue supernatants were fractionated on a discontinuous sucrose gradient developed to separate free and bound polyribosomes. Total RNA recovered averaged 3.2 mg/g tissue, 40% of which was with ER and 30% with the free polyribosomes, about 25% being with the postribosomal/RNP fraction. Slot-blot hybridization of equal portions of RNA revealed that 12 h after injection of turpentine to induce inflammation, ferritin mRNA was concentrated on the ER-bound polyribosomes, while it was concentrated on the free polyribosomes 2 h after injection of ferric ammonium citrate. Differences were highly significant, based on multiple determinations and densitometry. Profiles of ferritin mRNA distribution on linear sucrose gradients corroborated the differential findings. Concentrations of total ferritin mRNA per gram liver doubled with iron treatment but were not significantly different 12 h after turpentine treatment. At the same time point after turpentine, ferritin protein synthesis was increased twofold, as measured by the 1 h incorporation of [14C]leucine. We conclude that a significant portion of ferritin mRNA always associates with the ER-bound polyribosomes, and that inflammation and iron differentially alter the polysomal distribution of ferritin mRNA, suggesting that two different kinds of mRNA may be involved.

Animals↗
PubMed1980

Effect of adriamycin on the polyribosome and messenger-RNA content of rat heart muscle.

The myocardial contents of DNA, protein, total and polyribosomal RNA, messenger RNA (mRNA) and polyribosomes were determined in normal and adriamycin-treated rats. While the myocardial contents of DNA and protein changed only little in adriamycin-treated rats, total and polyribosomal RNA decreased by 23.2% and 35%, mRNA and polyribosomes by 51.6% and 38.7%. Size distribution and protein synthetic activity of the polyribosome preparations obtained remained unchanged in the adriamycin-treated rats. We conclude that the reduced myocardial contents of RNA, mRNA and polyribosomes cause the previously observed impairment of myocardial protein synthesis in adriamycin-treated rats and might be important in the pathogenesis of the adriamycin-cardiomyopathy.

Animals↗
PubMed1981

Acute effects of ethanol intake on albumin and total protein synthesis in free and membrane-bound polyribosomes of rat liver.

Controversial results have been reported in the last few years concerning the effects of ethanol on hepatic protein synthesis. In most of the studies no distinction has been made between the synthetic capabilities of the polyribosomes and the secretory product of labelled protein by the hepatocytes. In order to assess the influence of a single feeding of ethanol on the synthesis of albumin and total protein by the polyribosomes of rat liver, free and membrane-bound polyribosomes were isolated quantitatively from rats given 4--8 g ethanol per kg body weight 3--5 h before killing. The following results were obtained: (1) No difference was found in yield and size of free and membrane-bound polyribosomes isolated from control and ethanol-treated rats. The abilities to synthesize albumin and total protein were also equal for polyribosomes from both groups. (2) Addition of 1% ethanol to the incubation mixture of protein synthesis lowered albumin and total protein synthesis by 20%. No effect was observed with 0.5% ethanol. (3) Cell sap prepared from ethanol-treated rats contains a factor or factors which stimulate protein synthesis (10--15%). (4) The albumin mRNA sequence content was not changed in free and membrane-bound polyribosomal RNA fractions of ethanol-treated rats as compared to the control animals.

Animals↗
PubMed1977

Effect of aflatoxin B1 on hepatic polyribosomes and protein synthesis in the rat.

This study was concerned with the effect of aflatoxin B1 on protein synthesis in rat liver. Specifically, the effect of the administration of aflatoxin B1 (6.0 mg/kg body weight) on hepatic polyribosomes (free and membranebound), protein synthesis in vitro, and initiation factors activity of rats within 3-12 h was investigated. The results revealed that aflatoxin B1 rapidly led to disaggregation of free and membrane-bound polyribosomes, to inhibition of in vitro protein synthesis by both populations of polyribosomes, to little or no effect on the activities of initiation factors, and to defective ribosomes, particularly the 60S ribosomal subnits, of both types of polyribosomes. Comparative studies on the effects of aflatoxin B1 and actinomycin D revealed progressive disaggregation by both hepatic free and membrane-bound polyribosomes after aflatoxin B1 but not only of the free polyribosomes after actinomycin D.

Aflatoxins↗
PubMed1975

The mechanism of polyribosome disaggregation in brain tissue by phenylalanine.

The injection of neonatal mice with phenylalanine resulted in a rapid decrease in brain polyribosomes and a concomitant increase in monomeric ribosomes. Animals of 1-16 days of age were equally affected by phenylalanine, although the brain polyribosomes of 60-day-old mice were relatively resistant to the effects of phenylalanine. The population of free polyribosomes appeared to be more sensitive to phenylalanine treatment than bound polyribosomes, which were somewhat more resistant to disruption by high concentrations of the amino acid. The effects of phenylalanine were more pronounced with polyribosomes in the cerebral cortex than with those in the cerebellar tissue. The mechanism of polyribosome disruption was shown to be independent of hydrolysis mediated by ribonuclease. Virtually all of the monomeric ribosomes that resulted from phenylalanine treatment were shown to be inactive with regard to endogenous protein synthesis and were present in the cell cytoplasm as vacant couples. These ribosomes were readily dissociated by treatment with 0.5 M-KCl and subsequent ultracentrifugation. These results are discussed in the light of the possibility that high concentrations of phenylalanine disrupt brain protein synthesis by a molecular mechanism that is associated with initiation events.

Aging↗
PubMed1974

The 7S RNA common to oncornaviruses and normal cells is associated with polyribosomes.

The 7S RNA species first demonstrated in avian and murine oncornaviruses and later in normal, uninfected cells is found associated in part with cellular polyribosomes. A molar ratio of 7S RNA to 5S ribosomal RNA of 0.05 indicates that there is approximately one mole of 7S RNA per mole of messenger RNA. Dissociation of polyribosomes with dimethylsulfoxide results in a marked decrease in the sedimentation rate of the 7S RNA. The dimethylsulfoxide-induced dissociation of polyribosomes and the concomitant movement of the 7S RNA from the polyribosome region into lighter regions of a sucrose gradient are both inhibited by cycloheximide, indicating that the 7S RNA is indeed associated with polyribosomes and not with a ribonucleoprotein particle sedimenting with polyribosomes.

Animals↗
PubMed1977

Polyribosome distribution in regenerating livers of irradiated adrenalectomized rats.

The effect of gamma-radiation (1800 rad) on polyribosome distribution in the regenerating livers of intact and adrenalectomized rats was studied both before and after partial hepatectomy. The animals were divided into four sub-groups: (1) control; (2) irradiated only; (3) partially hepatectomized; and (4) irradiated partially hepatectomized. The relative distribution of lighter oligosomes to heavier polyribosomes was analysed by sucrose density gradient centrifugation (10-40 per cent). Partial hepatectomy by itself increased the proportion of heavier polyribosomes in both intact and adrenalectomized rats. However, when gamma-rays were delivered 2 hours before or 2 hours after partial-hepatectomy, the formation of heavy polyribosomes was decreased for at least 24 hours after hepatectomy in the adrenal intact rats. This depression was not maintained until later times (48 and 72 hours after hepatectomy) when an increase in the proportion of heavy polyribosomes relative to light oligosomes was observed. In addition, irradiation did not measurably affect the distribution of polyribosomes in regenerating hepatocytes of adrenalectomized rats at any time after partial hepatectomy.

Adrenalectomy↗
PubMed1964

ALTERATIONS IN POLYRIBOSOMES DURING ERYTHROID CELL MATURATION.

This communication presents a morphological study of the changes in ribosome content and organization which occur during the maturation of erythroid cells of the phenylhydrazine-treated rabbit. Electron micrographs of thin sectioned nucleated and non-nucleated erythroid cells have been subjected to a quantitative analysis of the distribution of ribosomes as polyribosomes of various sizes and as single ribosomes. The ribosomes of nucleated erythroid cells of marrow are virtually all arranged in the polyribosome configuration consisting of clusters of 2 to 6 individual ribosomes. These cells are the most active in the erythroid series in protein biosynthesis. During maturation to the non-nucleated reticulocyte stage, found in the circulating blood, there is a decrease in protein synthesizing capacity, a fall in total ribosome content, and, more significantly, a decrease in the number and size of polyribosomes. Maturation to the ribosome-free erythrocyte, either under in vitro or in vivo conditions, entails a further decrease in protein synthesis which correlates with a progressive disaggregation of the biosynthetically active polyribosomes into smaller clusters and inactive single ribosomes. Possible models which may account for the stability of the polyribosome and for the mechanism of polyribosome dissociation are discussed.

Animals↗