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PubMed1978

Asphyxia-induced disaggregation of cerebral polyribosomes in rhesus monkey fetuses.

The effects of 3 hours of controlled intrauterine asphyxia (acidotic hypoxia) on the sedimentation patterns of cerebral polyribosomes and on polyribosome supported in vitro protein synthesis were examined in 16 term monkey fetuses. Three outcomes resulted. Four fetuses showed no changes in polyribosome sedimentation profile or in sedimented polyribosome supported in vitro protein synthesis. Four showed changes in sedimentation profiles indicating partial breakdown of polyribosomes and significant decreases in polyribosome supported in vitro protein synthesis. Finally, 8 fetuses showed almost complete disaggregation of cerebral polyribosomes into 80-S monosomal units. This was associated with marked reduction in sedimented ribosomal mediated in vitro portein synthesis. Both the disaggregation of polyribosomes and the associated loss of in virto protein synthesis were related to the severity of the acidosis produced by asphyxia.

Animals↗
PubMed1976

[Isolation of preparative amounts of polyribosomes from normal rabbit and guinea pig spleen].

Preparative amounts of polyribosomes were isolated from normal rabbit and guinea pig spleen; up to 40 optical units of the polyribosome preparation could be obtained by centrifugation in a Spinco L-2B centrifuge with SW-27 rotor. The amount of polyribosomes isolated from spleens of immune animals was 2-3 higher than that isolated from normal animal spleens. Concentration of polyribosomal preparations by lyophylization and the storage of dried preparations do not alter the sedimentation properties of the polyribosomes. The distribution pattern of normal rabbit spleen polyribosomes in a linear sucrose gradient and the sedimentation constants of the polyribosome peaks are in good agreement with data reported by some other authors for plasmocytome polyribosomes. Using electrophoresis in agarose-polyacrylamide gel the radioactive proteins synthesized in the cell culture of normal rabbit spleen it was shown that in normal spleen the average amount of globulins makes up to 35% of total protein synthesis, as reported by some authors.

Animals↗
PubMed1976

[The activity of polynucleotide phosphorylase in polyribosomes of regenerating liver of adult rats, liver of newborn rats and in some reinoculated tumours].

Specific activity and level of polynucleotide phosphorylase (PNPase) in polyribosomes of regenerating liver of adult rats, liver of newborn rats and in malignant tumours of rat (sarcoma M-1 and hepatoma 27) were studied. 24 hours after partial hepatectomy the specific activity and level of PNPase in regenerating liver decreased 3--4 times in the fraction of polyribosomes, bound to the endoplasmic reticulum membranes, and remained at a constantly low level in the fraction of free polyribosomes. The PNPase activity also showed a sharp decrease in the fraction of membrane-bound polyribosomes from newborn rats liver and could not be detected either in free or in bound polyribosomes from sarcoma M-1 or hepatoma 27. The PNPase activity in the fraction of bound polyribosomes increased with a decrease in the rate of liver growth (regenerating liver and newborn rats liver), and reached the level normal for adult animals. Possible mechanisms of regulation of the PNPase activity in animal tissue were studied. It was found that a 2-fold administration of cyclic 3,5'-AMP to intact animals (5 mg per 100 g of body weight) with an interval of 8 hours, corresponding to the interval between two peaks of the increase in cyclic 3,5'-AMP concentration following partial hepatectomy, diminished the PNPase specific activity in polyribosomes by 30%. A factor, presumably of protein origin, which induced a release of PNPase from polyribosomes of normal rat liver but did not affect the activity of the liberated enzyme, was detected in the cell sap of sarcoma M-1 and hepatoma 27.

Age Factors↗
PubMed1980

[Properties of polyribosomal complexes of loach embryonic cell cytoplasm].

The translation-active complexes of the extranuclear region of cytoplasm of developing loach (Misgurnus fossilis) embryos were studied. The amount of ribosomes involved in polyribosomal complexes was shown to increase 6-fold from the blastula stage to organogenesis, making up only a small (3% and 18%, respectively) part of the total pool of cytoplasmic ribosomes. Free polyribosomes make up the bulk (up to 95%) of the total cytoplasmic polyribosomal pool at early stages of development (blastula, gastrula) and about 50% at late stages (organogenesis). The membrane-bound polyribosomes appear in early gastrulation; their content reaches its maximum (40-45%) in organogenesis. The newly formed RNAs liberated from the nucleus into the extranuclear space of the cytoplasm in the course of ontogenesis are incorporated into the polyribosomes (predominantly membrane-bound ones) not before the gastrulation starts. The proportion of these poly(A)-enriched mRNAs in the polyribosomes does not exceed 10% of the total amount of newly synthesized cytoplasmic RNAs at this stage. A population of light polyribosomes capable to synthesize histones was detected in free polyribosomes, which do not practically contain the newly formed RNAs. The data obtained are discussed in terms of the literary data on the type of RNA and protein synthesis in early ontogenesis.

Animals↗
PubMed1970

Electron microscopy of polyribosomes synthesizing immunoglobulin chains. Comparison with sizes determined by density-gradient-sedimentation data.

Polyribosomes from the immunoglobulin-producing plasma-cell tumour X5563 were fractionated on a linear sucrose gradient and fractions containing polyribosomes carrying heavy (H) and light (L) immunoglobulin chains were examined with the electron microscope. The size distribution of the polyribosomes in the various fractions was determined. The results are consistent with previous estimates by Williamson & Askonas (1967) of the size of the polyribosomes synthesizing immunoglobulin chains, despite some discrepancies in their calculations based on sedimentation data. In particular, polyribosomes of up to 18 ribosomes were present in the part of the gradient containing H-chain polyribosomes. The polyribosomal clusters appeared to be true linear aggregates of uniformly spaced ribosomes, arranged mostly in open or zig-zag configuration. The appearance of most of them does not seem to support a general helical model of the polyribosome.

Animals↗
PubMed1971

The association in vitro of polyribosomes with ribonuclease-treated derivatives of hepatic rough endoplasmic reticulum. Characteristics of the membrane binding sites and factors influencing association.

1. Pancreatic ribonuclease in dilute EDTA has been shown to condition rough-microsomal membranes from adult rat liver to accept exogenously added rat liver polyribosomes in vitro at 0-4 degrees C. Treated smooth membranes would not significantly interact with polyribosomes. 2. The conditioning process decreased the membrane RNA content and removed polyribosomes from vesicle surfaces as viewed electron-microscopically. 3. Binding to these conditioned membranes was shown to be uninfluenced by changes of temperature (0-37 degrees C) and pH (6.9-7.8) or the presence of cell sap, but was inhibited by increasing the concentration of potassium chloride. 4. Possession of a polyribosome-binding capacity by conditioned rough membranes was not dependent on adventitious materials that could be dislodged by high ionic strengths. 5. Trypsin treatment under mild conditions destroyed the binding capacity of ribonuclease-conditioned rough membranes. 6. A 2-10S residual RNA was recovered from ribonuclease-conditioned membranes, but its partial removal had no effect on the capacity of membranes to accept polyribosomes. However, some role for this residual RNA in attaching polyribosomes could not be discounted. 7. Evidence is considered that polyribosome-binding sites are intrinsic features of conditioned membranes isolated from rough-microsomal fractions, and that long-range ionic bonding is a primary factor in polyribosome interaction with these binding sites.

Amino Acids↗
PubMed1990

Evidence for increased translational efficiency in the induction of P450IIE1 by solvents: analysis of P450IIE1 mRNA polyribosomal distribution.

The potential for enhanced translational processing of P450IIE1 mRNA during the early phase of P450IIE1 induction by pyridine or acetone was assessed by hybridization analysis of polyribosomal P450IIE1 mRNA distribution in rat hepatic tissue. Optical absorbance profiles of polyribosomal fractions exhibited an apparent shift at 5 h following pyridine administration relative to control. Slot and Northern blot analyses for P450IIE1 mRNA in the cytoplasmic extracts isolated from 5 h pyridine-treated rats demonstrated a shift in distribution of P450IIE1 message toward heavier polyribosomal fractions and Northern blot analysis suggested the presence of different populations of P450IIE1 mRNA. Slot blot analyses also demonstrated a shift in the polyribosomal distribution of P450IIE1 mRNA at 12 h following pyridine treatment; in contrast, hybridization analysis for P450IA1 revealed no shift in polyribosomal distribution of P450IA1 mRNA. Acute acetone administration to animals also resulted in a similar shift in polyribosomal distribution of P450IIE1 mRNA as compared to control. These data suggest that P450IIE1 mRNA shifts toward larger polyribosomes following acute exposure of animals to pyridine or acetone and provide evidence that induction of P450IIE1 at early times following acute pyridine or acetone administration involves enhanced translational efficiency through increased loading of ribosomes on P450IIE1 mRNA.

Acetone↗
PubMed1975

Polyribosomal structures inactive for protein synthesis present in erythroid cells during terminal stages of differentiation.

During the terminal stages of differentiation nucleated erythroid cells from the fetal mouse synthesize hemoglobin at a lower rate because after the last cycle of cell division about half of their polyribosomal structures are rendered inactive for protien synthesis though they maintain their aggregated shape. Partially inactive polyribosomes are tested in comparison with normal polyribosomes for the capacity to support polypeptide chain synthesis in cell-free conditions. The following observations are made: a) no difference is found for the profile on sucrose density gradients; b) partially inactive polyribosomes carry growing polypeptide chains in reduced amounts in comparison with active polyribosomes; c) partially inactive polyribosomes are not capable to release "run off" 80 S ribosomal monomers and to dissociate to active ribosomal subunits. These data are interpreted as the evidence for a block of chain termination producing inactivation of polyribosomes during the late maturation of nucleated erythroid cells.

Animals↗
PubMed1984

The content and size distribution of membrane-bound and free polyribosomes in mouse liver during aging.

The method of Ramsey and Steele [Anal. Biochem., 92 (1979) 305--313] was used to examine the size distribution of membrane-bound and free polyribosomes from the liver of male C57 BL/6 mice over the life span. Optimization of the concentration of Mg2+ and liver cell sap suppressed breakdown by ribonuclease and presumably gave preparations that approximate the integrity of native polyribosome populations. The content of polysomes per unit liver tissue from 7 groups of fed mice aged 10--35 months showed an age-related increase of subunits and monomers (+54%) and dimers-to-pentamers (+76%) in membrane-bound polyribosomes. The dimer-to-pentamer class of free polyribosomes also increased (+52%). Polysomes larger than nonamers showed 13% and 21% decreases that were not statistically significant. Total tissue ribosomes increased 15%, while the membrane-bound/free polyribosome ratio remained nearly constant at about 1.15. In a subsequent study, both 6 h-fasted and fed mice showed decreases (-20% to -33%) in membrane-bound and free polyribosomes larger than nonamers during aging from 15 to 35 months. The dimer-to-pentamer class of free polyribosomes in fed mice increased (+26%), while this class in the other groups underwent increases (+26 to +39%) that were not statistically significant. We conclude that the liver in old mice is not obviously deficient in either quantity or general quality of ribosomes. Old animals do tend to show an increase in small polysomes and a decrease in large polysomes, which is consistent with a reduction in the rate of translation.

Aging↗
PubMed1973

Dietary protein intake and skeletal-muscle protein metabolism in rats. Studies with the ammonium chloride-wash fraction from crude polyribosomes of well-nourished and protein-depleted rats.

1. Crude polyribosomes from skeletal muscle of the hind leg of rats fed on a low-protein diet for 10 days are less active in cell-free protein synthesis than are polyribosomes obtained from well-nourished control rats. 2. The polyribosomes were salt-washed (0.5m-NH(4)Cl) and the wash extract was examined for its amino acid incorporating activity and for EF (elongation factor) 1 and EF 2 activities. 3. Compared with preparations from control rats, the salt-wash fraction from protein-depleted rats was less active and showed lower EF 1 and EF 2 activity. 4. The ribosomes were rendered equal in activity by salt-washing, but no inhibitor was detected in the salt wash. 5. Differences in the incorporating activity of crude polyribosomes from the diet groups persisted in the presence of saturating amounts of partially purified EF 1 and EF 2. 6. It is concluded that the lowered protein-synthetic activity of crude polyribosomes caused by restricted protein intake is not causally related to the lower activities of EF 1 and EF 2 in the polyribosome preparations. 7. The possible nature of the change in crude polyribosome activity due to low-protein feeding is discussed.

Amino Acids↗
PubMed1975

The effect of phenobarbitone on protein synthesis by liver polyribosomes in fed and starved rats.

1. The effect of phenobarbitone on the rate of protein synthesis and on the sedimentation patterns of various liver subcellular fractions containing ribosomes was studied in rats. 2. Phenobarbitone treatment increased the incorporation of [114C]leucine into protein by all preparations, provided they had not been subjected to preliminary treatment with Sephadex G-25. The phenobarbitone-induced effect on incorporation was associated with a gain in liver weight and a higher degree of polyribosomal aggregation. 3. Preparations that were treated with Sephadex G-25 incorporated more radioactivity into protein, but did not show the response to phenobarbitone treatment. 4. When the influence of starvation and phenobarbitone was studied separately on membrane-bound and membrane-free polyribosomes, it was shown that whereas both classes of polyribosomes were affected by starvation, apparently only the former class was susceptible to phenobarbitone stimulation of protein synthesis. 5. The decreased capacity for protein synthesis of polyribosomes from starved rats was independent of their association with the membranes of the endoplasmic reticulum, but resulted from polyribosomal disaggregation, from an intrinsic defect of the polyribosomes themselves and from changes in composition of the cell cap. 6. The results are discussed in relation to the problem of the control of protein biosynthesis and of the functional separation of membrane-bound and membrane-free polyribosomes.

Animals↗
PubMed1997

Relationship between yeast polyribosomes and Upf proteins required for nonsense mRNA decay.

In yeast, the accelerated rate of decay of nonsense mutant mRNAs, called nonsense-mediated mRNA decay, requires three proteins, Upf1p, Upf2p, and Upf3p. Single, double, and triple disruptions of the UPF genes had nearly identical effects on nonsense mRNA accumulation, suggesting that the encoded proteins function in a common pathway. We examined the distribution of epitope-tagged versions of Upf proteins by sucrose density gradient fractionation of soluble lysates and found that all three proteins co-distributed with 80 S ribosomal particles and polyribosomes. Treatment of lysates with RNase A caused a coincident collapse of polyribosomes and each Upf protein into fractions containing 80 S ribosomal particles, as expected for proteins that are associated with polyribosomes. Mutations in the cysteine-rich (zinc finger) and RNA helicase domains of Upf1p caused loss of function, but the mutant proteins remained polyribosome-associated. Density gradient profiles for Upf1p were unchanged in the absence of Upf3p, and although similar, were modestly shifted to fractions lighter than those containing polyribosomes in the absence of Upf2p. Upf2p shifted toward heavier polyribosome fractions in the absence of Upf1p and into fractions containing 80 S particles and lighter fractions in the absence of Upf3p. Our results suggest that the association of Upf2p with polyribosomes typically found in a wild-type strain depends on the presence and opposing effects of Upf1p and Upf3p.

Adaptor Proteins, Signal Transducing↗
PubMed1995

The majority of yeast UPF1 co-localizes with polyribosomes in the cytoplasm.

In Saccharomyces cerevisiae the UPF1 protein is required for nonsense-mediated mRNA decay, the accelerated turnover of mRNAs containing a nonsense mutation. Several lines of evidence suggest that translation plays an important role in the mechanism of nonsense mRNA decay, including a previous report that nonsense mRNAs assemble in polyribosomes. In this study we show that UPF1 and ribosomal protein L1 co-localize in the cytoplasm and that UPF1 co-sediments with polyribosomes. To detect UPF1, three copies of the influenza hemagglutinin epitope were placed at the C-terminus. The tagged protein, UPF1-3EP, retains 86% (+/- 5%) of function. Using immunological detection, we found that UPF1-3EP is primarily cytoplasmic and was not detected either in the nucleus or in the mitochondrion. UPF1-3EP and L1 co-distributed with polyribosomes fractionated in a 7-47% sucrose gradient. The sucrose sedimentation profiles for UPF1-3EP and L1 exhibited similar changes using three different sets of conditions that altered the polyribosome profile. When polyribosomes were disaggregated, UPF1-3EP and L1 accumulated in fractions coincident with 80S ribosomal particles. These results suggest that UPF1-3EP associates with polyribosomes. L3 and S3 mRNAs, which code for ribosomal proteins of the 60S and 40S ribosomal subunits, respectively, were on average about 100-fold more abundant than UPF1 mRNA. Assuming that translation rates for L3, S3, and UPF1 mRNA are similar, this result suggests that there are far fewer UPF1 molecules than ribosomes per cell. Constraints imposed by the low UPF1 abundance on the functional relationships between UPF1, polyribosomes, and nonsense mRNA turnover are discussed.

Base Sequence↗
PubMed1976

[The effect of cycloheximide on incorporation of newly formed mRNA into membrane-bound polyribosomes in rat liver cells].

Incorporation kinetics of new synthesized mRNA into free and endoplasmic membrane-bound polyribosomes in the absence of normal translation (when protein synthesis in inhibited by 98% with cycloheximide) is studied. mRNA is found to incorporate into both free and bound polyribosomes. Relative content of new synthesized membrane-bound polyribosomes in the presence of cycloheximide within 2.5-4.5 hours is by 30-40% lower as compared with the control. This fact can be explained either by the absence of a growing peptide of a sufficient length, which is necessary for the formation of a part of membrane-bound polyribosomes, or by a restricted number of attachment sites on membranes as a result of delayed translation of mRNA in pre-existed polyribosomes. It is suggested that 1) the growing peptide in liver cells is responsible for the recognition of a membrane only under the formation of only one type of membrane-bound polyribosomes, or 2) the formation of all bound polyribosomes has a single mechanism and the growing peptide does not participates in the membrane recognition.

Animals↗
PubMedDate not supplied

[Identification of transcortin-synthesizing polyribosomes in the rat liver].

Transcortin biosynthesis in rats has been examined using liver slices technique. The incorporation of [14C]-labelled amino acids into the anti-transcortin-precipitable material of liver slices has been measured and compared with that of serum transcortin. It was shown that liver synthesized transcortin with an apparent molecular weight of 66 kDa on SDS-electrophoresis which co-migrated with authentic rat serum transcortin. In order to determine an intracellular distribution of transcortin-synthesizing polyribosomes, the binding character of [125J] anti-transcortin-IgG to free and membrane-bound rat liver polyribosomes has been studied. It was shown that after incubation of [125J] anti-transcortin-IgG with liver membrane-bound polyribosomes, the radioactivity was associated with the discrete polyribosome fraction in the heavy polyribosome region. In similar experiments the radioactivity of [125J] anti-transcortin-IgG bound to free polyribosomes was distributed throughout the polyribosome region.

Animals↗
PubMedDate not supplied

[mRNA degradation in membrane-bound and free polyribosomes in rat liver cells after exposure to actinomycin D and cycloheximide].

Actinomycin D caused degradation of mRNA both in membrane-bound and in free polyribosomes from rat liver cells. The rate of mRNA destruction was distinctly higher in free polyribosomes, than in membrane-bound ones. Cycloheximide inhibited the mRNA destruction in both types of polyribosomes. At the same time, the stabilizing effect of cycloheximide on mRNA was less distinct in free polyribosomes. A decrease in specific radioactivity of mRNA from membrane-bound and free polyribosomes was observed after prolonged pretreatment with actinomycin D. The specific radioactivity of mRNA from polyribosomes of both types was not altered after simultaneous administration of actinomycin D and cycloheximide into rats. Occurence of two fractions of mRNA, dissimilar in stability, is possible both in membrane-bound and in free polyribosomes from rat liver cells.

Animals↗
PubMed1980

Tumor-immunotherapeutic efficacy of Serratia marcescens polyribosomes.

The ability of polyribosomes, obtained from several bacterial species, to suppress the development of cutaneous SaD2 fibrosarcomas in DBA/2 mice were evaluated. Suppression of tumor appearance depended upon the tumor load at the time of treatment, dose of polyribosomes, and species source of polyribosomes, with Serratia marcescens being superior to Escherichia coli, Streptococcus pneumoniae, Mycobacterium bovis (Pasteur), Mycobacterium smegmatis, and Propionibacterium acnes (formerly Corynebacterium parvum). A single injection of 5 or 50 microgram of Serratia polyribosomes at the tumor site 72 hr after the intradermal administration of 1.5 X 10(3) SaD2 cells resulted in 66 to 95% survival. All untreated animals expired within 50 days. Tumor suppression occurred at both flank and footpad sites. Presensitization with polyribosomes and incorporation of polyribosomes into adjuvant were not required for the tumor-suppressive effect. Treatment of Serratia polyribosomes with RNase or pronase reduced the number of survivors. Endotoxin was not detectable with the Limulus amebocyte lysate assay.

Animals↗
PubMed1978

[Stabilization of polyribosomal mRNA in rat liver cells under protein synthesis inhibition by cycloheximide].

It was found that in the course of centrifugation of the postmitochondrial fraction from rat liver in the sucrose concentration gradient, mRNA located in the EDTA-resistant structures sedimented together with polyribosomes. The same structures were detected in the polyribosomal fraction of liver cells after injection of ethionine to the animals. Centrifugation of polyribosomes through a layer of 2.0 M sucrose at 105 000 g for 4 hrs and subsequent centrifugation through a layer of 1.0 M sucrose resulted in the disappearance of the complexes from the polyribosomal fraction. Evidence for the absence of destruction of labelled polyribosomal mRNA in liver cells following the injection of cycloheximide were obtained. Actinomycin D also stabilized polyribosomal mRNA in liver cells, however, in a much lesser degree as compared to cycloheximide. Possible mechanisms of the stabilizing effects of cycloheximide and actinomycin D on polyribosomal mRNA in liver cells are discussed.

Animals↗