The Effect of Protein Synthesis Inhibition on the Entry of Messenger Rna Into the Cytoplasm of Sea Urchin Embryos

Hogan, Brigid; Gross, Paul R.

doi:10.1083/jcb.49.3.692

Cited by 80 publications

(20 citation statements)

References 24 publications

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“…Emetine is a potent specific inhibitor of protein synthesis in blastula and younger stages of sea urchin embryos (23). In this study it was also found that emetine is a specific and effective inhibitor of protein synthesis in older embryos.…”

Section: Discussionmentioning

confidence: 56%

“…The effect of inhibition of protein synthesis on the ontogenetic change in enzyme activity was determined. Emetine which had been shown to exert a specific inhibition of protein synthesis of young sea urchin embryos (23) was selected for this experiment. It was found that lo4 M emetine also effects specific inhibition of protein synthesis of post-gastrulation embryos.…”

Section: R Es U Ltsmentioning

confidence: 99%

See 1 more Smart Citation

Molecular Properties and Differentiation of Acetylcholinesterase in Sea Urchin Embryos*

Ozaki

1976

Dev Growth Differ

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The two molecular forms of acethylcholinesterase (EC 3.1.1.7) in sea urchin embryos were characterized by several physical methods. The sedimentation coefficients determined by sucrose gradient centrifugation are 7.6s and 10.6s. The Stokes radii determined by gel filtration are 65 a and 9 1 8. From these parameters, molecular weights were estimated as 190,000 and 380,000; the one is twice as large as the other. Both forms have similar electric property and buoyant density in a CsCl gradient. When the enzyme solution was concentrated, the 10.6s form became predominant. These results suggest that the two forms are monomer and dimer. The sea urchin enzymes resemble globular forms of acetylcholinesterase of the electric organ of fishes.The activity of the enzyme abruptly increases in post-gastrulation embryos. Inhibition of concomitant protein synthesis by a specific inhibitor, emetine, does not affect the increase in enzyme activity. The result suggests that post-translational processes may be involved in the differentiation of this enzyme in sea urchin development.The following sea urchins were used in the study: Strongylocentrotus purpuratus, Strongylocentrotus frunciscanus, and Dendruster excentricus.A marked increase in acetylcholinesterase activity occurs in post-gastrulation embryos o f the sea urchin (5, 39). Concomitantly, enzymes sensitive to an inhibitor of cholinesterase appear among the esterases resolved by polyacrylamide gel electrophoresis (37,38,40) and by immunoelectrophoresis (49). The enzyme activity is first localized in the mesenchyme cells of the young pluteus larva (39). The great increase in activity at a defined stage in development and its concentration in a specific region of the embryo make this system a useful model for the study of temporal and spatial controls of differentiation in early embryogenesis.Acetylcholinesterase of post-gastrulation sea urchin embryos exists in two forms in the supernatant fraction of the homogenate. The same two forms are present in the preparation of enzyme solubilized from the particulate fraction. Approximately 60% of the enzyme activity is associated with the particulate fraction. These two molecular forms have a similar electric property but differ in molecular size (39).In the present study, the two molecular forms were characterized further by several physical methods. The results show that the two forms are monomer and dimer, and that they resemble globular forms of acetylcholinesterase obtained from the electric organ of fishes (30). The present study, furthermore, demonstrates that ontogenetic changes in enzyme activity is not immediately dependent upon protein synthesis.

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Section: Discussionmentioning

confidence: 56%

Section: R Es U Ltsmentioning

confidence: 99%

Molecular Properties and Differentiation of Acetylcholinesterase in Sea Urchin Embryos*

Ozaki

1976

Dev Growth Differ

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“…This conclusion is based on the well-established effects of these protein synthesis inhibitors. The stabilization of polysomes in sea urchin embryos by treatment with the standard concentration of emetine has been demonstrated previously (27,28), as has the dissociation of polysomes by pactamycin at standard concentrations (17). To eliminate the possibility that colcemid treatment alters the action of these protein synthesis inhibitors, we analyzed the polysome profiles of embryos that were treated simultaneously with colcemid and one of these inhibitors.…”

Section: Resultsmentioning

confidence: 98%

“…Inhibition of protein synthesis in plutei had little effect on the prevalence of tubulin RNA (Fig. 3) (27,28) and pactamycin (17) at the concentrations used in this investigation. Moreover, in this investigation we confirmed the effects of these inhibitors on polysomes of embryos treated with colcemid and observed that tubulin mRNA behaves in the same way as the general population of mRNA in embryos treated with these agents.…”

Section: Resultsmentioning

confidence: 99%

Stabilization of tubulin mRNA by inhibition of protein synthesis in sea urchin embryos.

Gong¹,

Brandhorst²

1988

Mol. Cell. Biol.

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An increased level of unpolymerized tubulin caused by depolymerization of microtubules in sea urchin larvae resulted in a rapid loss of tubulin mRNA, which was prevented by nearly complete inhibition of protein synthesis. Results of an RNA run-on assay indicated that inhibition of protein synthesis does not alter tubulin gene transcription. Analysis of the decay of tubulin mRNA in embryos in which RNA synthesis was inhibited by actinomycin D indicated that inhibition of protein synthesis prevents the destabilization of tubulin mRNA. The effect was similar whether mRNA was maintained on polysomes in the presence of emetine or anisomycin or displaced from the polysomes in the presence of puromycin or pactamycin; thus, the stabilization of tubulin mRNA is not dependent on the state of the polysomes after inhibition of protein synthesis. Even after tubulin mRNA declined to a low level after depolymerization of microtubules, it could be rescued by treatment of embryos with inhibitors of protein synthesis. Tubulin mRNA could be induced to accumulate prematurely in gastrulae but not in plutei if protein synthesis was inhibited, an observation that is indicative of the importance of the autogenous regulation of tubulin mRNA stability during embryogenesis. Possible explanations for the role of protein synthesis in the control of mRNA stability are discussed.

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“…Thus, by monitoring polyribosomes in the presence and absence of these drugs, limitations at this initiation step can be identified. We used emetine to study initiation as it is more effective than cycloheximide in inhibiting protein synthesis in sea urchin embryos (Hogan and Gross, 1971) and in reticulocytes, presumably because of a difference in uptake (Lodish, 1971). …”

Section: Treatment With Emetinementioning

confidence: 99%

Translational control in sea urchin eggs and embryos: Initiation is rate limiting in blastula stage embryos

Hille

Hall

Yablonka–Reuveni

et al. 1981

Developmental Biology

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To determine whether initiation is rate-limiting in protein synthesis during the embryogenesis of sea urchins, polyribosome profiles of unfertilized eggs and cleavage, blastula and prism stage embryos were examined after incubation of the eggs and embryos in the presence and absence of low amounts of emetine, an inhibitor of polypeptide elongation. The ribosomes were radioactively labeled with [ 3 H]uridine by injection of the adults during oogenesis so that we could monitor emetine-dependent shifts of monoribosomes to polyribosomes. Although initiation is not rate limiting in unfertilized eggs or 2-to 16-cell embryos of Strongylocentrotus purpuratus, it is rate limiting in blastula and prism embryos. We suggest that initiation becomes rate limiting to allow the selective translation of certain classes of mRNA during later development.

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The Effect of Protein Synthesis Inhibition on the Entry of Messenger Rna Into the Cytoplasm of Sea Urchin Embryos

Abstract: INTRODUCTION

Cited by 80 publications

References 24 publications

Molecular Properties and Differentiation of Acetylcholinesterase in Sea Urchin Embryos*

Molecular Properties and Differentiation of Acetylcholinesterase in Sea Urchin Embryos*

Stabilization of tubulin mRNA by inhibition of protein synthesis in sea urchin embryos.

Translational control in sea urchin eggs and embryos: Initiation is rate limiting in blastula stage embryos

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