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1

Wang, Houping, Jason B. Dictenberg, Li Ku, Wen Li, Gary J. Bassell, and Yue Feng. "Dynamic Association of the Fragile X Mental Retardation Protein as a Messenger Ribonucleoprotein between Microtubules and Polyribosomes." Molecular Biology of the Cell 19, no. 1 (January 2008): 105–14. http://dx.doi.org/10.1091/mbc.e07-06-0583.

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The fragile X mental retardation protein (FMRP) is a selective RNA-binding protein that regulates translation and plays essential roles in synaptic function. FMRP is bound to specific mRNA ligands, actively transported into neuronal processes in a microtubule-dependent manner, and associated with polyribosomes engaged in translation elongation. However, the biochemical relationship between FMRP–microtubule association and FMRP–polyribosome association remains elusive. Here, we report that although the majority of FMRP is incorporated into elongating polyribosomes in the soluble cytoplasm, microtubule-associated FMRP is predominantly retained in translationally dormant, polyribosome-free messenger ribonucleoprotein (mRNP) complexes. Interestingly, FMRP–microtubule association is increased when mRNPs are dynamically released from polyribosomes as a result of inhibiting translation initiation. Furthermore, the I304N mutant FMRP that fails to be incorporated into polyribosomes is associated with microtubules in mRNP particles and transported into neuronal dendrites in a microtubule-dependent, 3,5-dihydroxyphenylglycine-stimulated manner with similar kinetics to that of wild-type FMRP. Hence, polyribosome-free FMRP–mRNP complexes travel on microtubules and wait for activity-dependent translational derepression at the site of function. The dual participation of FMRP in dormant mRNPs and polyribosomes suggests distinct roles of FMRP in dendritic transport and translational regulation, two distinct phases that control local protein production to accommodate synaptic plasticity.
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2

Zalewski, Kazimierz. "The metabolism of aged seeds. The formation of polyribosomes in germinating field bean ( Vicia faba sp. minor) seeds of different ages." Acta Societatis Botanicorum Poloniae 61, no. 2 (2014): 203–10. http://dx.doi.org/10.5586/asbp.1992.018.

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Total dehydrogenase activity and formation of polyribosomes in embryonic axes and cotyledons of field bean seeds from different harvest years were studied. <sup>3</sup>H-uridine incorporation experiments showed that seed ageing was accompanied by decreased capability for RNA synthesis and polyribosome formation. The embryonic axes of seeds with reduced vigor contained lower levels of polyribosomes.
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3

Ma, Xinrong, Fadia Ibrahim, Eun-Jeong Kim, Scott Shaver, James Becker, Fareha Razvi, Ronald L. Cerny, and Heriberto Cerutti. "An ortholog of the Vasa intronic gene is required for small RNA-mediated translation repression inChlamydomonas reinhardtii." Proceedings of the National Academy of Sciences 117, no. 1 (December 23, 2019): 761–70. http://dx.doi.org/10.1073/pnas.1908356117.

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Small RNAs (sRNAs) associate with Argonaute (AGO) proteins in effector complexes, termed RNA-induced silencing complexes (RISCs), which regulate complementary transcripts by translation inhibition and/or RNA degradation. In the unicellular algaChlamydomonas, several metazoans, and land plants, emerging evidence indicates that polyribosome-associated transcripts can be translationally repressed by RISCs without substantial messenger RNA (mRNA) destabilization. However, the mechanism of translation inhibition in a polyribosomal context is not understood. Here we show thatChlamydomonasVIG1, an ortholog of theDrosophila melanogasterVasa intronic gene (VIG), is required for this process. VIG1 localizes predominantly in the cytosol and comigrates with monoribosomes and polyribosomes by sucrose density gradient sedimentation. AVIG1-deleted mutant shows hypersensitivity to the translation elongation inhibitor cycloheximide, suggesting that VIG1 may have a nonessential role in ribosome function/structure. Additionally, FLAG-tagged VIG1 copurifies with AGO3 and Dicer-like 3 (DCL3), consistent with it also being a component of the RISC. Indeed, VIG1 is necessary for the repression of sRNA-targeted transcripts at the translational level but is dispensable for cleavage-mediated RNA interference and for the association of the AGO3 effector with polyribosomes or target transcripts. Our results suggest that VIG1 is an ancillary ribosomal component and plays a role in sRNA-mediated translation repression of polyribosomal transcripts.
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4

Boissonneault, Guylain, and Roland R. Tremblay. "Combined use of oligo(dt) and 28S cDNA probes for the quantitation of total mRNA in polyribosomes: Application to the castration-induced atrophy of the rat prostate." Bioscience Reports 10, no. 2 (April 1, 1990): 179–88. http://dx.doi.org/10.1007/bf01116577.

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The castration-induced atrophy of the rat prostate was used as a model for the validation of a sensitive technique allowing the quantitation of total mRNA in polyribosomes. Electron micrographs of polyribosome samples showed a decrease in polyribosomes length 7 days after castration (GDX). Specificity of labeled oligo(dt) probe for poly(A) was demonstrated and the technique was successfully applied to demonstrate that GDX is associated with a decrease in poly(A) mRNA content of polyribosomes. Provided that normalization of the hybridization signal for mRNA is achieved with a rRNA cDNA probe, the assay therefore represents a suitable tool for further studies regarding the translational regulation of total and/or specific mRNAs.
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5

Zalewski, Kazimierz. "Possible role of growth regulators in adaptation to heat stress affecting partitioning of photosynthates in tomato plants." Acta Societatis Botanicorum Poloniae 58, no. 1 (2014): 85–95. http://dx.doi.org/10.5586/asbp.1989.007.

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The formation of polyribosomes and total dehydrogenase activity in rye grains from different harvest years (with different viability) were studied. It was found using actinomycin D and cordycepin that grain aging was related to a lower ability for RNA synthesis and polyribosome formation. At least part of the stored form of RNA (preformed mRNA) in the embryos of both aged non-viable grain was able to form complexes with ribosomes.
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6

Greenland, Andrew, and Michael Shaw. "Polyribosome fractions and protein synthesis in stem rust infected wheat." Canadian Journal of Botany 64, no. 9 (September 1, 1986): 1916–27. http://dx.doi.org/10.1139/b86-255.

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The effects of infection by stem-rust fungus on polyribosomal RNA fractions and protein synthesis in vitro and in vivo in near-isogenic resistant (Sr6) and susceptible (sr6) lines of wheat were determined. In infected resistant leaves the proportion of ribosomes present as polyribosomes was greater than that in healthy (uninfected) leaves at 1, 3, and 6 days and that in susceptible leaves at 1 and 3 days after inoculation. In the latter there were large increases in the pelletable RNA content (ribosomes, ribosomal subunits, and polyribosomes) and proportion of ribosomes present as polyribosomes from day 6. In vitro translation failed to detect any marked differences in polyribosomal translation products in resistant and susceptible leaves in response to infection. Labelling of polypeptides in vivo and separation by one- and two-dimensional electrophoresis showed that at 1 day after inoculation, two groups of high molecular mass polypeptides (80–96 and 100–110 kDa) were more heavily labelled and two novel polypeptides were present in resistant and susceptible leaves in response to infection. Synthesis of the high molecular weight and two novel polypeptides was maintained in infected resistant leaves up to 6 days after inoculation. In susceptible leaves the amount of radiolabel incorporated into these polypeptides and several proteins prominently labelled in uninfected controls declined rapidly from 3 days after inoculation.
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7

Wang, Y. "High-throughput polyribosome fractionation." Nucleic Acids Research 32, no. 10 (June 2, 2004): e79-e79. http://dx.doi.org/10.1093/nar/gnh077.

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8

Weidner, Stanisław, Włodzimierz Makowski, and Andrzej Rejowski. "The use of transcription inhibitors in the study of the mechanism of abscisic acid action in germinating triticale caryopses." Acta Societatis Botanicorum Poloniae 56, no. 3 (2014): 455–67. http://dx.doi.org/10.5586/asbp.1987.043.

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The study was conducted on germinating triticale (var. Grado) caryopses. The purpose of the experiments was to compare the effect of selected inhibitors of transcription with the action of abscisic acid during germination of caryopses. The following inhibitors were used: α-amanitin, cordycepin, cycloheximide and 5-fluorouracil. Studied were the synthesis of total and polyribosomal RNA, the process of polyribosome formation and the synthesis of ribosomal proteins. The effect of exogenous ABA, especially in the early stages of germination, was not similar to any of the four above inhibitors of transcription. After 12 h of imbibition at a lowered temperature and 3 h of germination, ABA caused a relatively low level of inhibition of RNA synthesis, whereas all of the inhibitors used halted RNA synthesis in embryos by about 50-60%. After 6 h of germination, the same proportion of polyribosomes in the total ribosome fraction (46%) was found in both the embryos from the control sample and treated with ABA. The use of inhibitors brought this figure down to below 40%. The conclusion is drawn that in the early stages of germination, regulation of protein synthesis by ABA in triticale caryopses must occur on a level other than transcription.
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9

Yost, Christian C., Melvin M. Denis, Stephan Lindemann, Frederick J. Rubner, Gopal K. Marathe, Michael Buerke, Thomas M. McIntyre, Andrew S. Weyrich, and Guy A. Zimmerman. "Activated Polymorphonuclear Leukocytes Rapidly Synthesize Retinoic Acid Receptor-α." Journal of Experimental Medicine 200, no. 5 (August 30, 2004): 671–80. http://dx.doi.org/10.1084/jem.20040224.

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In addition to releasing preformed granular proteins, polymorphonuclear leukocytes (PMNs) synthesize chemokines and other factors under transcriptional control. Here we demonstrate that PMNs express an inducible transcriptional modulator by signal-dependent activation of specialized mechanisms that regulate messenger RNA (mRNA) translation. HL-60 myelocytic cells differentiated to surrogate PMNs respond to activation by platelet activating factor by initiating translation and with appearance of specific mRNA transcripts in polyribosomes. cDNA array analysis of the polyribosome fraction demonstrated that retinoic acid receptor (RAR)-α, a transcription factor that controls the expression of multiple genes, is one of the polyribosome-associated transcripts. Quiescent surrogate HL60 PMNs and primary human PMNs contain constitutive message for RAR-α but little or no protein. RAR-α protein is rapidly synthesized in response to platelet activating factor under the control of a specialized translational regulator, mammalian target of rapamycin, and is blocked by the therapeutic macrolide rapamycin, events consistent with features of the 5′ untranslated region of the transcript. Newly synthesized RAR-α modulates production of interleukin-8. Rapid expression of a transcription factor under translational control is a previously unrecognized mechanism in human PMNs that indicates unexpected diversity in gene regulation in this critical innate immune effector cell.
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10

Atkin, A. L., N. Altamura, P. Leeds, and M. R. Culbertson. "The majority of yeast UPF1 co-localizes with polyribosomes in the cytoplasm." Molecular Biology of the Cell 6, no. 5 (May 1995): 611–25. http://dx.doi.org/10.1091/mbc.6.5.611.

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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.
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11

Atkinson, Burr G., Ling Liu, Ing Swie Goping, and David B. Walden. "Expression of the genes encoding hsp73, hsp18, and ubiquitin in radicles of heat-shocked maize seedlings." Genome 31, no. 2 (January 15, 1989): 698–704. http://dx.doi.org/10.1139/g89-127.

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Radicles of intact 5-day-old maize (cv. OH43) seedlings exposed to a rapid, short-term elevation (2 h) in environmental (25 to 42.5 °C) temperature exhibit new and (or) enhanced synthesis of a specific set of proteins, the so-called heat shock proteins (hsps), with molecular masses of 108 000, 89 000, 84 000, 76 000, 73 000, 30 000, 23 000, and 18 000. Continuous exposure of intact seedlings to this elevated temperature results in a depression in the synthesis of these hsps after 8 – 12 h and a shift in the pattern of the proteins synthesized to one that resembles those proteins synthesized by radicles from seedlings grown at 25 °C. The transient synthesis of hsp73 and the hsp18 family in radicles from seedlings exposed to, and maintained at, an elevated temperature correlates with the levels of hsp73 and hsp18 mRNAs associated with their polyribosomes. The heat shock induced accumulation of these hsp mRNAs occurs concomitantly with a fourfold increase in polyribosome-associated ubiquitin mRNAs. However, unlike the transient association of hsp73 and hsp18 mRNAs with polyribosomes in radicles from seedlings maintained at 42.5 °C (8 – 12 h), the level of uniquitin mRNAs associated with polyribosomes does not return to a steady-state control (25 °C) level for at least 24 h. The marked, rapid increase in the level of ubiquitin mRNAs associated with polyribosomes in radicles from heat-shocked seedlings provides the first evidence implicating ubiquitin as a heat shock protein of plants.Key words: heat Shock, heat shock proteins, ubiquitin, maize.
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12

Pleština, Stjepko, and Stjepan Gamulin. "Kidney Ischaemia-Reperfusion Injury and Polyribosome Structure." Nephron 89, no. 2 (2001): 201–7. http://dx.doi.org/10.1159/000046068.

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13

Spirin, Alexander S., and Murat A. Ajtkhozhin. "Informosomes and polyribosome-associated proteins in eukaryotes." Trends in Biochemical Sciences 10, no. 4 (April 1985): 162–65. http://dx.doi.org/10.1016/0968-0004(85)90158-6.

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14

Molenaars, Marte, Georges E. Janssens, Toon Santermans, Marco Lezzerini, Rob Jelier, Alyson W. MacInnes, and Riekelt H. Houtkooper. "Mitochondrial ubiquinone–mediated longevity is marked by reduced cytoplasmic mRNA translation." Life Science Alliance 1, no. 5 (August 31, 2018): e201800082. http://dx.doi.org/10.26508/lsa.201800082.

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Mutations in the clk-1 gene impair mitochondrial ubiquinone biosynthesis and extend the lifespan in Caenorhabditis elegans. We demonstrate here that this life extension is linked to the repression of cytoplasmic mRNA translation, independent of the alleged nuclear form of CLK-1. Clk-1 mutations inhibit polyribosome formation similarly to daf-2 mutations that dampen insulin signaling. Comparisons of total versus polysomal RNAs in clk-1(qm30) mutants reveal a reduction in the translational efficiencies of mRNAs coding for elements of the translation machinery and an increase in those coding for the oxidative phosphorylation and autophagy pathways. Knocking down the transcription initiation factor TATA-binding protein-associated factor 4, a protein that becomes sequestered in the cytoplasm during early embryogenesis to induce transcriptional silencing, ameliorates the clk-1 inhibition of polyribosome formation. These results underscore a prominent role for the repression of cytoplasmic protein synthesis in eukaryotic lifespan extension and suggest that mutations impairing mitochondrial function are able to exploit this repression similarly to reductions of insulin signaling. Moreover, this report reveals an unexpected role for TATA-binding protein-associated factor 4 as a repressor of polyribosome formation when ubiquinone biosynthesis is compromised.
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15

Weidner, Stanisław. "Studies on the mechanism which prevents germination of unripe Triticale caryopses." Acta Societatis Botanicorum Poloniae 53, no. 3 (2014): 325–37. http://dx.doi.org/10.5586/asbp.1984.029.

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<em>Triticale</em> (MT-3) caryopses were collected at three developmental stages (milk, milk-wax, and full ripeness i.e. 25, 39, 53 days after flowering) and germinated for 72 hours. The highest polyribosome contribution to the sum total of ribosomes, as well as, the highest <sup>3</sup>H-uridine incorporation into the total ribosomal fraction of embryos (seedlings) were found at full ripeness, lower - at milk ripeness, and the lowest at milk-wax ripeness. Treatment of caryopses with gibberellin-A<sub>3</sub> (GA<sub>3</sub>) and benzyloadenine (BA) caused an increase in the percentage of embryonic polyribosomes in caryopses which were collected at milk and full ripeness. Whereas the significant increase in <sup>3</sup>H-uridine incorporation intothe total ribosomal fractions of embryos (seedlings) was observed only during the germination of the least ripe caryopses. This was characteristic of samples with caryopses at milk ripeness treated with BA, or BA and GA<sub>3</sub> together. The studies proved that the mechanism which prevents the germination of unripe Triticale cyryopses and the formation of polyribosomes which were germination-induced, originated at the final stage of grain development, before its full ripeness.
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16

Pleština, S., and S. Gamulin. "Mouse kidney polyribosome structure during ischaemia-reperfusion injury." Pathophysiology 5 (June 1998): 59. http://dx.doi.org/10.1016/s0928-4680(98)80506-3.

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17

Ohya, Toshihide, and Hiroshi Suzuki. "Cytokinin-promoted Polyribosome Formation in Excised Cucumber Cotyledons." Journal of Plant Physiology 133, no. 3 (October 1988): 295–98. http://dx.doi.org/10.1016/s0176-1617(88)80203-7.

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18

MacLennan, P. A., and M. J. Rennie. "Effects of ischaemia, blood loss and reperfusion on rat muscle protein synthesis, metabolite concentrations and polyribosome profiles in vivo." Biochemical Journal 260, no. 1 (May 15, 1989): 195–200. http://dx.doi.org/10.1042/bj2600195.

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In adult rat gastrocnemius muscles, on reperfusion after 45 min of tourniquet ischaemia, protein synthetic rates were depressed by over half for 1 h compared to normal (12%/day), and were at least one-third below normal for up to 5 h afterwards. Ischaemia caused muscle concentrations of phosphocreatine to be depressed by 70%, and those of lactate to be elevated by 350%; the proportion of ribosomes as polyribosomes was decreased by half. Unlike the rates of protein synthesis, all of these variables returned to normal after 35 min of reperfusion. When 25% of the blood volume was removed (for 10-45 min), there were falls in the rate of gastrocnemius protein synthesis and in phosphocreatine concentration, and an increase in lactate concentration. On blood replacement, protein synthesis and metabolite concentrations returned to normal within 15 min. Polyribosome profiles were unaffected by blood loss or replacement. There were highly significant correlations between the rate of gastrocnemius protein synthesis and both phosphocreatine concentration and 1/(lactate concentration), during blood loss and replacement, i.e. during both the fall and rise in muscle energy status. We conclude that the effects of ischaemia and blood loss on protein synthesis are not equivalent.
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19

Ulovec, Z., P. Narancsik, and S. Gamulin. "Effects of Hypoglycemia on Rat Brain Polyribosome Sedimentation Pattern." Journal of Neurochemistry 45, no. 2 (August 1985): 352–54. http://dx.doi.org/10.1111/j.1471-4159.1985.tb03995.x.

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20

Desjardins, Pierre, Chantal Savoie, Johanne Doucet, and Didier Gauthier. "Isolation and characterization of hamster brain polyribosome-cytomatrix complexes." Neurochemistry International 21, no. 1 (July 1992): 21–27. http://dx.doi.org/10.1016/0197-0186(92)90064-x.

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21

Bond, Andrew T., David A. Mangus, Feng He, and Allan Jacobson. "Absence of Dbp2p Alters Both Nonsense-Mediated mRNA Decay and rRNA Processing." Molecular and Cellular Biology 21, no. 21 (November 1, 2001): 7366–79. http://dx.doi.org/10.1128/mcb.21.21.7366-7379.2001.

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ABSTRACT Dbp2p, a member of the large family of DEAD-box proteins and a yeast homolog of human p68, was shown to interact with Upf1p, an essential component of the nonsense-mediated mRNA decay pathway. Dbp2p:Upf1p interaction occurs within a large conserved region in the middle of Upf1p that is largely distinct from its Nmd2p and Sup35/45p interaction domains. Deletion of DBP2, or point mutations within its highly conserved DEAD-box motifs, increased the abundance of nonsense-containing transcripts, leading us to conclude that Dbp2p also functions in the nonsense-mediated mRNA decay pathway. Dbp2p, like Upf1p, acts before or at decapping, is predominantly cytoplasmic, and associates with polyribosomes. Interestingly, Dbp2p also plays an important role in rRNA processing. In dbp2Δ cells, polyribosome profiles are deficient in free 60S subunits and the mature 25S rRNA is greatly reduced. The ribosome biogenesis phenotype, but not the mRNA decay function, of dbp2Δ cells can be complemented by the human p68 gene. We propose a unifying model in which Dbp2p affects both nonsense-mediated mRNA decay and rRNA processing by altering rRNA structure, allowing specific processing events in one instance and facilitating dissociation of the translation termination complex in the other.
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22

Mawn, Mary V., Maurille J. Fournier, David A. Tirrell, and Thomas L. Mason. "Depletion of Free 30S Ribosomal Subunits in Escherichia coli by Expression of RNA Containing Shine-Dalgarno-Like Sequences." Journal of Bacteriology 184, no. 2 (January 15, 2002): 494–502. http://dx.doi.org/10.1128/jb.184.2.494-502.2002.

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ABSTRACT We have constructed synthetic coding sequences for the expression of poly(α,l-glutamic acid) (PLGA) as fusion proteins with dihydrofolate reductase (DHFR) in Escherichia coli. These PLGA coding sequences use both GAA and GAG codons for glutamic acid and contain sequence elements (5′-GAGGAGG-3′) that resemble the consensus Shine-Dalgarno (SD) sequence found at translation initiation sites in bacterial mRNAs. An unusual feature of DHFR-PLGA expression is that accumulation of the protein is inversely related to the level of induction of its mRNA. Cellular protein synthesis was inhibited >95% by induction of constructs for either translatable or untranslatable PLGA RNAs. Induction of PLGA RNA resulted in the depletion of free 30S ribosomal subunits and the appearance of new complexes in the polyribosome region of the gradient. Unlike normal polyribosomes, these complexes were resistant to breakdown in the presence of puromycin. The novel complexes contained 16S rRNA, 23S rRNA, and PLGA RNA. We conclude that multiple noninitiator SD-like sequences in the PLGA RNA inhibit cellular protein synthesis by sequestering 30S small ribosomal subunits and 70S ribosomes in nonfunctional complexes on the PLGA mRNA.
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23

Park, Young-Un, Hyangsuk Hur, Minhan Ka, and Jinmi Kim. "Identification of Translational Regulation Target Genes during Filamentous Growth in Saccharomyces cerevisiae: Regulatory Role of Caf20 and Dhh1." Eukaryotic Cell 5, no. 12 (October 13, 2006): 2120–27. http://dx.doi.org/10.1128/ec.00121-06.

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ABSTRACT The dimorphic transition of yeast to the hyphal form is regulated by the mitogen-activated protein kinase and cyclic AMP-dependent protein kinase A pathways in Saccharomyces cerevisiae. Signaling pathway-responsive transcription factors such as Ste12, Tec1, and Flo8 are known to mediate filamentation-specific transcription. We were interested in investigating the translational regulation of specific mRNAs during the yeast-to-hyphal-form transition. Using polyribosome fractionation and RT-PCR analysis, we identified STE12, GPA2, and CLN1 as translation regulation target genes during filamentous growth. The transcript levels for these genes did not change, but their mRNAs were preferentially associated with polyribosomes during the hyphal transition. The intracellular levels of Ste12, Gpa2, and Cln1 proteins increased under hyphal-growth conditions. The increase in Ste12 protein level was partially blocked by mutations in the CAF20 and DHH1 genes, which encode an eIF4E inhibitor and a decapping activator, respectively. In addition, the caf20 and dhh1 mutations resulted in defects in filamentous growth. The filamentation defects caused by caf20 and dhh1 mutations were suppressed by STE12 overexpression. These results suggest that Caf20 and Dhh1 control yeast filamentation by regulating STE12 translation.
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24

Pérez-Sala, D., R. Parrilla, and M. S. Ayuso. "Key role of l-alanine in the control of hepatic protein synthesis." Biochemical Journal 241, no. 2 (January 15, 1987): 491–98. http://dx.doi.org/10.1042/bj2410491.

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We investigated the effects of administration of single amino acids to starved rats on the regulation of protein synthesis in the liver. Of all the amino acids tested, only alanine, ornithine and proline promoted statistically significant increases in the extent of hepatic polyribosome aggregation. The most effective of these was alanine, whose effect of promoting polyribosomal aggregation was accompanied by a decrease in the polypeptide-chain elongation time. The following observations indicate that alanine plays an important physiological role in the regulation of hepatic protein synthesis. Alanine was the amino acid showing the largest decrease in hepatic content in the transition from high (fed) to low (starved) rates of protein synthesis. The administration of glucose or pyruvate is also effective in increasing liver protein synthesis in starved rats, and their effects were accompanied by an increased hepatic alanine content. An increase in hepatic ornithine content does not lead to an increased protein synthesis, unless it is accompanied by an increase of alanine. The effect of alanine is observed either in vivo, in rats pretreated with cycloserine to prevent its transamination, or in isolated liver cells under conditions in which its metabolic transformation is fully impeded.
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25

Caruccio, N., and J. Ross. "Purification of a human polyribosome-associated 3‘ to 5‘ exoribonuclease." Journal of Biological Chemistry 269, no. 50 (December 1994): 31814–21. http://dx.doi.org/10.1016/s0021-9258(18)31768-x.

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26

Dunn, James C. Y., Joseph S. Friedberg, Ronald C. Tompkins, and Martin L. Yarmush. "Hepatocytes From Rat Liver Perfusions Physicochemical Effects on Polyribosome Size." ASAIO Journal 38, no. 4 (October 1992): 841–45. http://dx.doi.org/10.1097/00002480-199210000-00019.

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27

Weidner, Stanisław, Włodzimierz Makowski, Eugeniusz Sójka, and Andrzej Rejowski. "The role of zeatin and gibberellic acid in breaking of the abscisic acid-induced dormancy in Triticale caryopses." Acta Societatis Botanicorum Poloniae 53, no. 3 (2014): 339–51. http://dx.doi.org/10.5586/asbp.1984.030.

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The investigations were conducted on the germinating embryos and the whole caryopses of <em>Triticale</em>. During preimbibition and 24 hours germination caryopses were treated with abscisic acid (ABA), which produced 63% inhibition of embryo growth. Gibberellin-A<sub>3</sub> (GA<sub>3</sub>) reversed the ABA effect in 18%, while zeatin in 22%. The clear synergic reaction was observed (36%) when both stimulators acted together. There was no significant effect of ABA, ABA and GA<sub>3</sub>, as well as ABA and zeatin on the synthesis of polyribosomal RNA in the initial period of germination of excised embryos. However, during 24 hours germination of whole caryopses ABA caused a twofold decrease in <sup>3</sup>H-uridine incorporation into the total fraction of embryonic ribosomes. While the incorporation of <sup>14</sup>C-aminoacid mixture into ribosomal proteins was even three-fold lower. Effect of GA<sub>3</sub> and zeatin on breaking of the ABA-induced "dormancy" was studied. It was confirmed that the higher polyribosome contribution to the sum total of ribosomes the more intensive synthesis of ribosomal proteins. No higher <sup>3</sup>H-uridine incorporation into polyribosomal fraction was observed. From the results it may be inferred that in the initial period of germination of <em>Triticale</em> caryopses regulation of protein biosynthesis occurs rather at the translation than transcription level.
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28

Stephens, Samuel B., Rebecca D. Dodd, Joseph W. Brewer, Patrick J. Lager, Jack D. Keene, and Christopher V. Nicchitta. "Stable Ribosome Binding to the Endoplasmic Reticulum Enables Compartment-specific Regulation of mRNA Translation." Molecular Biology of the Cell 16, no. 12 (December 2005): 5819–31. http://dx.doi.org/10.1091/mbc.e05-07-0685.

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In eukaryotic cells, protein synthesis is compartmentalized; mRNAs encoding secretory/membrane proteins are translated on endoplasmic reticulum (ER)-bound ribosomes, whereas mRNAs encoding cytosolic proteins are translated on free ribosomes. mRNA partitioning between the two compartments occurs via positive selection: free ribosomes engaged in the translation of signal sequence-encoding mRNAs are trafficked from the cytosol to the ER. After translation termination, ER-bound ribosomes are thought to dissociate, thereby completing a cycle of mRNA partitioning. At present, the physiological basis for termination-coupled ribosome release is unknown. To gain insight into this process, we examined ribosome and mRNA partitioning during the unfolded protein response, key elements of which include suppression of the initiation stage of protein synthesis and polyribosome breakdown. We report that unfolded protein response (UPR)-elicited polyribosome breakdown resulted in the continued association, rather than release, of ER-bound ribosomes. Under these conditions, mRNA translation in the cytosol was suppressed, whereas mRNA translation on the ER was sustained. Furthermore, mRNAs encoding key soluble stress proteins (XBP-1 and ATF-4) were translated primarily on ER-bound ribosomes. These studies demonstrate that ribosome release from the ER is termination independent and identify new and unexpected roles for the ER compartment in the translational response to induction of the unfolded protein response.
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29

Sattlegger, Evelyn, and Alan G. Hinnebusch. "Polyribosome Binding by GCN1 Is Required for Full Activation of Eukaryotic Translation Initiation Factor 2α Kinase GCN2 during Amino Acid Starvation." Journal of Biological Chemistry 280, no. 16 (February 18, 2005): 16514–21. http://dx.doi.org/10.1074/jbc.m414566200.

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The protein kinase GCN2 mediates translational control of gene expression in amino acid-starved cells by phosphorylating eukaryotic translation initiation factor 2α. InSaccharomyces cerevisiae,activation of GCN2 by uncharged tRNAs in starved cells requires its direct interaction with both the GCN1·GCN20 regulatory complex and ribosomes. GCN1 also interacts with ribosomes in cell extracts, but it was unknown whether this activity is crucial for its ability to stimulate GCN2 function in starved cells. We describe point mutations in two conserved, noncontiguous segments of GCN1 that lead to reduced polyribosome association by GCN1·GCN20 in living cells without reducing GCN1 expression or its interaction with GCN20. Mutating both segments simultaneously produced a greater reduction in polyribosome binding by GCN1·GCN20 and a stronger decrease in eukaryotic translation initiation factor 2α phosphorylation than did mutating in one segment alone. These findings provide strong evidence that ribosome binding by GCN1 is required for its role as a positive regulator of GCN2. A particular mutation in the GCN1 domain, related in sequence to translation elongation factor 3 (eEF3), decreased GCN2 activation much more than it reduced ribosome binding by GCN1. Hence, the eEF3-like domain appears to have an effector function in GCN2 activation. This conclusion supports the model that an eEF3-related activity of GCN1 influences occupancy of the ribosomal decoding site by uncharged tRNA in starved cells.
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30

Sheets, M. D., B. Fritz, R. S. Hartley, and Y. Zhang. "Polyribosome analysis for investigating mRNA translation in Xenopus oocytes, eggs and embryos." Methods 51, no. 1 (May 2010): 152–56. http://dx.doi.org/10.1016/j.ymeth.2010.01.023.

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31

Adjibade, Pauline, Valerie Grenier St-Sauveur, Arnaud Droit, Edouard W. Khandjian, Paul Toren, and Rachid Mazroui. "Analysis of the translatome in solid tumors using polyribosome profiling/RNA-Seq." Journal of Biological Methods 3, no. 4 (November 21, 2016): 59. http://dx.doi.org/10.14440/jbm.2016.151.

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32

Steward, Oswald, Paula M. Falk, and Enrique R. Torre. "Ultrastructural basis for gene expression at the synapse: synapse-associated polyribosome complexes." Journal of Neurocytology 25, no. 1 (January 1996): 717–34. http://dx.doi.org/10.1007/bf02284837.

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33

Templin, Andrew T., Bernhard Maier, Sarah A. Tersey, Masayuki Hatanaka, and Raghavendra G. Mirmira. "Maintenance of Pdx1 mRNA Translation in Islet β-Cells During the Unfolded Protein Response." Molecular Endocrinology 28, no. 11 (November 1, 2014): 1820–30. http://dx.doi.org/10.1210/me.2014-1157.

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In type 1 diabetes, proinflammatory cytokines secreted by infiltrating immune cells activate the unfolded protein response (UPR) in islet β-cells, which leads to attenuation of global mRNA translation. Under such conditions, privileged mRNAs required for adaptation to the prevailing stress are maintained in an actively translated state. Pdx1 is a β-cell transcription factor that is required for the adaptive UPR, but it is not known how translation of its mRNA is maintained under these conditions. To study translation, we established conditions in vitro with MIN6 cells and mouse islets and a mixture of proinflammatory cytokines (IL-1β, TNF-α, and IFN-γ) that mimicked the UPR conditions seen in type 1 diabetes. Cell extracts were then subjected to polyribosome profiling to monitor changes to mRNA occupancy by ribosomes. Similar to other privileged mRNAs (Atf4 and Chop), Pdx1 mRNA remained partitioned in actively translating polyribosomes under the UPR, whereas the mRNA encoding a proinsulin-processing enzyme (Cpe) and others partitioned into inactively translating monoribosomes. Bicistronic luciferase reporter analyses revealed that the distal portion of the 5′-untranslated region of mouse Pdx1 (between bp −105 to −280) contained elements that promoted translation under both normal and UPR conditions, and this region exhibited conserved sequences and secondary structure similar to those of other known internal ribosome entry sites. Our findings suggest that Pdx1 protein levels are maintained in the setting of the UPR, in part, through elements in the 5′-untranslated region that confer privileged mRNA translation in a 5′-7-methylguanylate cap–independent manner.
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34

Gwóźdź, Edward A., and Grzegorz Jackowski. "Quantitative Stimulation of Polyribosome-dependent Translation by Microsomal Membranes from Developing Lupin Cotyledons." Biochemie und Physiologie der Pflanzen 181, no. 7 (January 1986): 467–73. http://dx.doi.org/10.1016/s0015-3796(86)80036-1.

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35

Hansen, P. E., E. Lied, and T. Børresen. "Estimation of protein synthesis in fish larvae using an in vitro polyribosome assay." Aquaculture 79, no. 1-4 (July 1989): 85–89. http://dx.doi.org/10.1016/0044-8486(89)90448-1.

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36

Wernerman, Jan, Alexandra von der Decken, and Erik Vinnars. "Polyribosome concentration in human skeletal muscle after starvation and parenteral or enteral refeeding." Metabolism 35, no. 5 (May 1986): 447–51. http://dx.doi.org/10.1016/0026-0495(86)90136-8.

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37

Lied, E., and A. von der Decken. "Purification of fish muscle myosin heavy chain and quantification of the specific polyribosome-bound polypeptide." Biochemical Journal 232, no. 2 (December 1, 1985): 467–70. http://dx.doi.org/10.1042/bj2320467.

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A purification procedure for fish myosin heavy chain is described. The protein was injected into rabbits for production of antibodies. The specificity of the antibodies was determined by immunoblotting. The enzyme-linked immunosorbent assay technique was applied to quantify myosin heavy chain bound to isolated polyribosomes of epaxial muscle from fish.
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38

Liu, Ling, Daniel S. Maillet, J. Roger H. Frappier, David B. Walden, and Burr G. Atkinson. "Characterization, chromosomal mapping, and expression of different polyubiquitin genes in tissues from control and heat-shocked maize seedlings." Biochemistry and Cell Biology 73, no. 1-2 (January 1, 1995): 19–30. http://dx.doi.org/10.1139/o95-003.

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Polyubiquitin transcripts accumulate in plant and animal cells following a heat shock. Most species have a few to several polyubiquitin genes; within a species, the genes may differ in nucleotide (nt) sequence and (or) the number of 228-nt repeats encoding the ubiquitin monomer. This study examines three maize (inbred Oh43) polyubiquitin genes. Two of the genes, MubG9 and MubG5, possess five repeats; the third, MubG1 possesses seven repeats. Sequence analyses of the genomic clones, MubG9 and MubG1 and a cDNA clone, MubG5, reveal that they differ primarily from each other in their nt sequences 5′ and 3′ to their open reading frames. MubG1 contains a 1004-base pair (bp) intron in its 5′ untranslated region. Using gene-specific probes, we show that the amount of polyribosome-associated mRNA transcripts from MubG9 isolated from 2- and 5-day old plumules and radicles is unchanged by heat shock. While the amount of transcript from MubG1 and MubG5 on the polyribosomes in plumules and radicles of 2-day-old seedlings is also unchanged by heat shock, the levels of these transcripts are elevated considerably in similar tissues from heat-shocked 5-day-old seedlings. Similar or identical gene-specific probes were employed to map the genes using the recombinant inbred method. MubG9 maps to chromosome 4L position 186; MubG1 maps to 5L104 and MubG5 to 4L188. The opportunity to use gene-specific probes extends the evidence for distinct modulation (time and tissue) of polyubiquitin gene expression in maize and provides the basis for locus assignment within the genome.Key words: ubiquitin, maize, heat shock, heat-shock proteins, gene expression, chromosome map.
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39

Krowczynska, A., and G. Brawerman. "Structural features in the 3'-terminal region of polyribosome-bound rabbit globin messenger RNAs." Journal of Biological Chemistry 261, no. 1 (January 1986): 397–402. http://dx.doi.org/10.1016/s0021-9258(17)42486-0.

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40

Singh, U. N. "Polyribosome Dynamics: Size-Distribution as a Function of Attachment, Translocation and Release of Ribosomes." Journal of Theoretical Biology 179, no. 2 (March 1996): 147–59. http://dx.doi.org/10.1006/jtbi.1996.0055.

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41

Sidell, Neil, Yue Feng, Lijuan Hao, Juanjuan Wu, Jie Yu, Maureen A. Kane, Joseph L. Napoli, and Robert N. Taylor. "Retinoic Acid Is a Cofactor for Translational Regulation of Vascular Endothelial Growth Factor in Human Endometrial Stromal Cells." Molecular Endocrinology 24, no. 1 (January 1, 2010): 148–60. http://dx.doi.org/10.1210/me.2009-0155.

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Abstract Vascular endothelial growth factor (VEGF) and endometrial angiogenesis play a critical role in successful embryonic implantation. Despite many studies of the effects of estrogen and progesterone on VEGF expression, its focal regulation at the site of implantation is unknown. Retinoic acid (RA) has been reported to regulate VEGF in a variety of cell types. Because localized RA synthesis occurs within the periimplantation endometrium, we tested the possibility that RA regulates VEGF production in endometrial stromal cells. Using primary and telomerase-immortalized human endometrial stromal cells, we determined that RA alone did not alter constitutive levels of VEGF production, but markedly amplified secretion when the cells were cotreated with activators of VEGF gene transcription (12-O-tetradecanoyl phorbol-13-acetate, TPA; TGF-β; and IL-1β). Whereas TPA or TGF-β alone stimulated VEGF promoter activity and up-regulated mRNA levels, significant protein secretion was detected only after RA was added to the culture systems. Analysis of retinoids in secretory phase endometrial biopsies indicated that endogenous RA accumulated at concentrations sufficient to induce VEGF secretion. Polyribosome profile analysis showed that the addition of RA to transcriptional activators of VEGF shifted the translational suppressed VEGF mRNA transcripts into larger polyribosome complexes engaged in active translation. Although the precise mechanism(s) of the RA effect remains to be defined, it appears to be mediated by reactive oxygen species; the antioxidant N-acetylcysteine inhibited RA+TPA-stimulated secretion of VEGF by more than 80%. Together, our results demonstrate that in human endometrial stromal cells, RA can combine with transcriptional activators of VEGF to augment VEGF secretion through a translational mechanism of action mediated by reactive oxygen species. These findings suggest a link between the spatiotemporal changes of retinoid synthesis in the periimplantation stroma and the capacity to quickly up-regulate focal VEGF secretion needed to induce early angiogenic events of pregnancy.
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42

Petracek, Marie E., Lynn F. Dickey, Steven C. Huber, and William F. Thompson. "Light-Regulated Changes in Abundance and Polyribosome Association of Ferredoxin mRNA Are Dependent on Photosynthesis." Plant Cell 9, no. 12 (December 1997): 2291. http://dx.doi.org/10.2307/3870586.

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43

Yang, Feng, and Daniel R. Schoenberg. "Endonuclease-Mediated mRNA Decay Involves the Selective Targeting of PMR1 to Polyribosome-Bound Substrate mRNA." Molecular Cell 14, no. 4 (May 2004): 435–45. http://dx.doi.org/10.1016/j.molcel.2004.05.001.

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44

Petracek, M. E., L. F. Dickey, S. C. Huber, and W. F. Thompson. "Light-regulated changes in abundance and polyribosome association of ferredoxin mRNA are dependent on photosynthesis." Plant Cell 9, no. 12 (December 1997): 2291–300. http://dx.doi.org/10.1105/tpc.9.12.2291.

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45

Mason, H. S., and K. Matsuda. "Polyribosome metabolism, growth and water status in the growing tissues of osmotically stressed plant seedlings." Physiologia Plantarum 64, no. 1 (May 1985): 95–104. http://dx.doi.org/10.1111/j.1399-3054.1985.tb01218.x.

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46

Nipper, Rick W., Vargheese Chennothukuzhi, Levent Tutuncu, Carmen J. Williams, George L. Gerton, and Stuart B. Moss. "Differential RNA expression and polyribosome loading of alternative transcripts of theAkap4 gene in murine spermatids." Molecular Reproduction and Development 70, no. 4 (2005): 397–405. http://dx.doi.org/10.1002/mrd.20224.

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47

Sherameti, Irena, Masayaki Nakamura, Yoshiharu Y. Yamamoto, Thomas Pfannschmidt, Junichi Obokata, and Ralf Oelmüller. "Polyribosome loading of spinach mRNAs for photosystem I subunits is controlled by photosynthetic electron transport." Plant Journal 32, no. 5 (December 2002): 631–39. http://dx.doi.org/10.1046/j.1365-313x.2002.01452.x.

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48

Ostroff, Linnaea E., Deborah J. Watson, Guan Cao, Patrick H. Parker, Heather Smith, and Kristen M. Harris. "Shifting patterns of polyribosome accumulation at synapses over the course of hippocampal long-term potentiation." Hippocampus 28, no. 6 (April 16, 2018): 416–30. http://dx.doi.org/10.1002/hipo.22841.

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49

Wang, Chunfu, Jill Pflugheber, Rhea Sumpter, Donald L. Sodora, Daniel Hui, Ganes C. Sen, and Michael Gale. "Alpha Interferon Induces Distinct Translational Control Programs To Suppress Hepatitis C Virus RNA Replication." Journal of Virology 77, no. 7 (April 1, 2003): 3898–912. http://dx.doi.org/10.1128/jvi.77.7.3898-3912.2003.

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ABSTRACT Hepatitis C virus (HCV) infection is treated with interferon (IFN)-based therapy. The mechanisms by which IFN suppresses HCV replication are not known, and only limited efficacy is achieved with therapy because the virus directs mechanisms to resist the host IFN response. In the present study we characterized the effects of IFN action upon the replication of two distinct quasispecies of an HCV replicon whose encoded NS5A protein exhibited differential abilities to bind and inhibit protein kinase R (PKR). Metabolic labeling experiments revealed that IFN had little overall effect upon HCV protein stability or polyprotein processing but specifically blocked translation of the HCV RNA, such that the replication of both viral quasispecies was suppressed by IFN treatment of the Huh7 host cells. However, within cells expressing an NS5A variant that inhibited PKR, we observed a reduced level of eukaryotic initiation factor 2 alpha subunit (eIF2α) phosphorylation and a concomitant increase in HCV protein synthetic rates, enhancement of viral RNA replication, and a partial rescue of viral internal ribosome entry site (IRES) function from IFN suppression. Assessment of the ribosome distribution of the HCV replicon RNA demonstrated that the NS5A-mediated block in eIF2α phosphorylation resulted in enhanced recruitment of the HCV RNA into polyribosome complexes in vivo but only partially rescued the RNA from polyribosome dissociation induced by IFN treatment. Examination of cellular proteins associated with HCV-translation complexes in IFN-treated cells identified the P56 protein as an eIF3-associated factor that fractionated with the initiator ribosome-HCV RNA complex. Importantly, we found that P56 could independently suppress HCV IRES function both in vitro and in vivo, but a mutant P56 that was unable to bind eIF3 had no suppressive action. We conclude that IFN blocks HCV replication through translational control programs involving PKR and P56 to, respectively, target eIF2- and eIF3-dependent steps in the viral RNA translation initiation process.
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50

Hamill, D., J. Davis, J. Drawbridge, and K. A. Suprenant. "Polyribosome targeting to microtubules: enrichment of specific mRNAs in a reconstituted microtubule preparation from sea urchin embryos." Journal of Cell Biology 127, no. 4 (November 15, 1994): 973–84. http://dx.doi.org/10.1083/jcb.127.4.973.

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A subset of mRNAs, polyribosomes, and poly(A)-binding proteins copurify with microtubules from sea urchin embryos. Several lines of evidence indicate that the interaction of microtubules with ribosomes is specific: a distinct stalk-like structure appears to mediate their association; ribosomes bind to microtubules with a constant stoichiometry through several purification cycles; and the presence of ribosomes in these preparations depends on the presence of intact microtubules. Five specific mRNAs are enriched with the microtubule-bound ribosomes, indicating that translation of specific proteins may occur on the microtubule scaffolding in vivo.
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