scholarly journals Specific mRNA destabilization in Dictyostelium discoideum requires RNA synthesis.

1987 ◽  
Vol 7 (12) ◽  
pp. 4585-4588 ◽  
Author(s):  
J F Amara ◽  
H F Lodish
Keyword(s):  
Protein Synthesis ◽  
Dictyostelium Discoideum ◽  
Rna Synthesis ◽  
Protein Synthesis Inhibitors ◽  
Protein And Rna Synthesis ◽  
The Common ◽  
Mrna Destabilization ◽  
Actin Protein ◽  
Specific Mrna

We tested the effects of inhibitors of protein and RNA synthesis on the disaggregation-mediated destabilization of prespore mRNAs in Dictyostelium discoideum. Incubating disaggregated cells with daunomycin to inhibit RNA synthesis prevented the loss of prespore mRNAs, whereas the inhibitor decreased or did not affect levels of the common mRNAs CZ22 and actin. Protein synthesis inhibitors varied in their effects. Cycloheximide, which inhibited protein synthesis almost completely, prevented the loss of the prespore mRNAs, but puromycin, which inhibited protein synthesis less well, did not. These results indicate that the process of specific mRNA destabilization requires the synthesis of RNA and possibly of protein.

Specific mRNA destabilization in Dictyostelium discoideum requires RNA synthesis

1987 ◽  
Vol 7 (12) ◽  
pp. 4585-4588
Author(s):  
J F Amara ◽  
H F Lodish
Keyword(s):  
Protein Synthesis ◽  
Dictyostelium Discoideum ◽  
Rna Synthesis ◽  
Protein Synthesis Inhibitors ◽  
Protein And Rna Synthesis ◽  
The Common ◽  
Mrna Destabilization ◽  
Actin Protein ◽  
Specific Mrna

We tested the effects of inhibitors of protein and RNA synthesis on the disaggregation-mediated destabilization of prespore mRNAs in Dictyostelium discoideum. Incubating disaggregated cells with daunomycin to inhibit RNA synthesis prevented the loss of prespore mRNAs, whereas the inhibitor decreased or did not affect levels of the common mRNAs CZ22 and actin. Protein synthesis inhibitors varied in their effects. Cycloheximide, which inhibited protein synthesis almost completely, prevented the loss of the prespore mRNAs, but puromycin, which inhibited protein synthesis less well, did not. These results indicate that the process of specific mRNA destabilization requires the synthesis of RNA and possibly of protein.

scholarly journals Analysis of specific mRNA destabilization during Dictyostelium development

Development ◽  
1989 ◽  
Vol 106 (3) ◽  
pp. 473-481
Author(s):  
G. Mangiarotti ◽  
S. Bulfone ◽  
R. Giorda ◽  
P. Morandini ◽  
A. Ceccarelli ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Dictyostelium Discoideum ◽  
Rna Synthesis ◽  
Actinomycin D ◽  
Secondary Effect ◽  
Cell Dissociation ◽  
Specific Mrnas ◽  
Mrna Destabilization ◽  
Selection Of ◽  
Specific Mrna

A number of specific mRNAs are destabilized upon disaggregation of developing Dictyostelium discoideum cells. Analysis of a family of cloned genes indicates that only prespore-enriched mRNAs are affected; constitutive mRNAs that are expressed throughout development and mRNAs that accumulate preferentially in prestalk cells are stable under these conditions. The decay of sensitive prespore mRNAs can be halted by allowing the cells to reaggregate, indicating that destabilization occurs by the progressive selection of individual molecules rather than on all members of an mRNA subpopulation at the time of disaggregation. Individual molecules of the sensitive mRNA species remain engaged in protein synthesis in the disaggregated cells until selected. Destabilization of sensitive mRNAs is induced by cell dissociation even in the presence of concentrations of nogalamycin that inhibit RNA synthesis. The reported prevention of disaggregation-induced mRNA decay by actinomycin D and daunomycin is therefore probably a secondary effect unrelated to the inhibition of transcription.

Biotin and glucose metabolism

1970 ◽  
Vol 48 (4) ◽  
pp. 493-500 ◽  
Author(s):  
K. Dakshinamurti ◽  
L. Tarrago-Litvak ◽  
Ho Chong Hong
Keyword(s):  
Protein Synthesis ◽  
Glucose Metabolism ◽  
Pyruvate Kinase ◽  
Rna Synthesis ◽  
De Novo ◽  
Diabetic Rat ◽  
Bifunctional Enzyme ◽  
Protein And Rna Synthesis ◽  
Rat Experiments ◽  
De Novo Protein Synthesis

Biotin enhances liver glucokinase in the diabetic rat. Experiments using inhibitors of protein and RNA synthesis suggest that this is mediated through de novo protein synthesis. Biotin treatment also increases the activities of other key glycolytic kinases, phosphofructokinase and pyruvate kinase, but has no effect on a bifunctional enzyme like phosphohexose isomerase.

Metabolic requirements for interactions between nuclear and cytoplasmic membranes in the repair of damaged Amoeba nuclei

1976 ◽  
Vol 21 (2) ◽  
pp. 291-302
Author(s):  
C.J. Flickinger
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Synthesis ◽  
Membrane Fusion ◽  
Energy Production ◽  
Rna Synthesis ◽  
Metabolic Inhibitors ◽  
Protein Synthesis Inhibitors ◽  
Nuclear Membranes ◽  
Cytoplasmic Membranes ◽  
Rna And Protein Synthesis

Amoeba nuclear envelopes were damaged using microsurgery, and metabolic requirements for the steps in their repair were studied, and my placing the cells in a solution containing one of several metabolic inhibitors. The first step in repair, the association of pieces of endoplasmic reticulum with holes in the nuclear membranes, appears to be a passive process since it was not affected by inhibitors of energy production, RNA synthesis, or protein synthesis. In contrast, fusion of pieces of endoplasmic reticulum with the nuclear membranes at the margins of the holes was blocked by KCN and dinitrophenol, indicating that membrane fusion requires energy derived from respiration, but RNA and protein synthesis inhibitors did not prevent fusion of pieces of endoplasmic reticulum with the nuclear membranes. The subsequent completion of repair and restoration of intact nuclear membranes was almost completely blocked by inhibitors of respiration, and it was reduced in the presence of actinomycin and emetine, suggesting that in addition to a requirement for energy, some later steps in the repair of the nuclear membranes require RNA and protein synthesis.

scholarly journals PROTEIN SYNTHESIS AND RNA SYNTHESIS DURING MITOSIS IN ANIMAL CELLS

1963 ◽  
Vol 19 (2) ◽  
pp. 267-277 ◽  
Author(s):  
Carol G. Konrad
Keyword(s):  
Protein Synthesis ◽  
Messenger Rna ◽  
Rna Synthesis ◽  
Animal Cells ◽  
Drastic Reduction ◽  
Human Amnion ◽  
Culture Cells ◽  
Cent Increase ◽  
Protein And Rna Synthesis ◽  
Synthetic Capacity

Protein synthesis and RNA synthesis during mitosis were studied by autoradiography on mammalian tissue culture cells. Protein synthesis was followed by incubating hamster epithelial and human amnion cells for 10 or 15 minutes with phenylalanine-C14. To study RNA synthesis the hamster cells were incubated for 10 minutes with uridine-C14. Comparisons of the synthetic capacity of the interphase and mitotic cells were then made using whole cell grain counts. The rate of RNA synthesis decreased during prophase and reached a low of 13 to 16 per cent of the average interphase rate during metaphase-anaphase. Protein synthesis in the hamster cells showed a 42 per cent increase during prophase with a subsequent return to the average interphase value during metaphase-anaphase. The human amnion cells showed no significant change at prophase but there was a 52 to 56 per cent drop in phenylalanine incorporation at metaphase-anaphase as compared to the average interphase rate. Colcemide was used on the hamster cells to study the effect of a prolonged mitotic condition on protein and RNA synthesis. Under this condition, uridine incorporation was extremely low whereas phenylalanine incorporation was still relatively high. The drastic reduction of RNA synthesis observed under mitotic conditions is believed to be due to the coiled condition of the chromosomes. The lack of a comparable reduction in protein synthesis during mitosis is interpreted as evidence for the presence in these cells of a relatively stable messenger RNA.

Effects of protein synthesis inhibitors during reactivation of associative memory in the common snail induces reversible and irreversible amnesia

2007 ◽  
Vol 37 (9) ◽  
pp. 921-928 ◽  
Author(s):  
S. V. Solntseva ◽  
V. P. Nikitin ◽  
S. A. Kozyrev ◽  
A. V. Shevelkin ◽  
A. V. Lagutin ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Associative Memory ◽  
Common Snail ◽  
Protein Synthesis Inhibitors ◽  
The Common

Inhibition of protein synthesis by zinc: comparison between protein synthesis and RNA synthesis

1998 ◽  
Vol 17 (12) ◽  
pp. 661-667 ◽  
Author(s):  
Udo Ingbert Walther ◽  
Johannes Schulze ◽  
Wolfgang Forth
Keyword(s):  
Protein Synthesis ◽  
Rna Synthesis ◽  
A549 Cells ◽  
Zinc Toxicity ◽  
Alveolar Type ◽  
Time Curve ◽  
Synthesis Inhibition ◽  
Protein And Rna Synthesis ◽  
Rna And Protein Synthesis

Inhalation of zinc fumes may lead to the acute respiratory distress syndrome. The mechanisms of pulmonary zinc toxicity are not yet understood. Therefore we investigated zinc-dependent depression of protein and RNA synthesis in rat and human lung cell lines. 1 After exposure to 120 or 150 mmol/l zinc, RNA synthesis as assessed by uridine incorporation decreased by 60-70% between 0 and 2 h exposition in rat alveolar type II cells (L2 cells) and human fibroblast-like cells (11Lu and 16Lu cells), and by 90% between 0 and 4 h in carcinoma-derived cells (A549 cells). 2 After 2 h exposure, L2, 11Lu, and 16Lu cells were half-maximally inhibited by 50 mmol/l zinc, whereas A549 cells were more resistant with half-maximal inhibition at 100 mmol/zinc. 3 Protein and RNA synthesis was inhibited in parallel in L2, 11Lu, and A549 cells as indicated by simultaneous determination of uridine and amino acid incorporation. In 16Lu cells, the decline in protein synthesis preceded RNA synthesis inhibition. Pretreatment with RNA synthesis inhibitors (amanitin or actinomycin D) had no effect on time curve and intensity of RNA synthesis inhibition. Taken together, our results indicate that the suppression of RNA and protein synthesis likely are independent phenomena, due to direct zinc effects on these biosynthetic pathways.

scholarly journals SYNTHESIS OF PLASMA MEMBRANE-ASSOCIATED AND SECRETORY IMMUNOGLOBULIN IN DIPLOID LYMPHOCYTES

1972 ◽  
Vol 135 (1) ◽  
pp. 136-149 ◽  
Author(s):  
Richard A. Lerner ◽  
Patricia J. McConahey ◽  
Inga Jansen ◽  
Frank J. Dixon
Keyword(s):  
Cell Cycle ◽  
Protein Synthesis ◽  
Plasma Membrane ◽  
Rna Synthesis ◽  
Actinomycin D ◽  
G1 Phase ◽  
Synchronized Cells ◽  
Disappearance Time ◽  
Protein And Rna Synthesis ◽  
Secretory Immunoglobulin

The half disappearance time for detectable plasma membrane-associated and cytoplasmic immunoglobulin after treatment of continuously growing diploid lymphocytes with inhibitors of protein and RNA synthesis was studied. Also, the amount of plasma membrane-associated and cytoplasmic immunoglobulin of synchronized cells in the G1 phase of the cell cycle has been studied. Plasma membrane-associated immunoglobulin has a half disappearance time of 45 min after inhibition of protein synthesis. By contrast, after treatment of cells with actinomycin D for 24 hr, plasma membrane-associated immunoglobulin remains relatively unchanged whereas cytoplasmic immunoglobulin decreased by almost 90%. In the G1 phase of the cell cycle, plasma membrane-associated immunoglobulin and cytoplasmic immunoglobulin were 70 and 10%, respectively, of that in logarithmically growing cells, and the half disappearance of M-Ig after treatment of cells with puromycin was again 45 min. In toto, these results suggest that perhaps secreted and plasma membrane-associated immunoglobulin may be separately controlled by the cells.

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