Induction of Drug-Metabolizing Enzymes and Ribosomal Protein Synthesis During Actinomycin Blockage of Ribonucleic Acid Synthesis

1974 ◽  
Vol 2 (6) ◽  
pp. 1357-1358
Author(s):  
JOHN G. NIEVEL
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Ribonucleic Acid ◽  
Acid Synthesis ◽  
Drug Metabolizing Enzymes ◽  
Metabolizing Enzymes ◽  
Ribosomal Protein Synthesis

scholarly journals Hierarchy of elements regulating synthesis of ribosomal proteins in Saccharomyces cerevisiae.

1981 ◽  
Vol 1 (11) ◽  
pp. 1016-1023 ◽  
Author(s):  
D R Kief ◽  
J R Warner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Ribonucleic Acid ◽  
Ribosomal Proteins ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Messenger Ribonucleic Acid ◽  
Ribosomal Protein Synthesis ◽  
Stimulation Of

Saccharomyces cerevisiae cells respond to a heat shock by temporarily slowing the synthesis of ribosomal proteins (C. Gorenstein and J. R. Warner, Proc. Natl. Acad. Sci. U.S.A. 73:1574-1551, 1976). When cultures growing oxidatively on ethanol as the sole carbon source were shifted from 23 to 36 degrees C, the synthesis of ribosomal proteins was coordinately inhibited twice as rapidly and 45% more severely than in comparable cultures growing fermentatively on glucose. Within 15 min, the relative rates of synthesis of at least 30 ribosomal proteins declined to less than one-sixth their initial values, whereas the overall rate of protein synthesis increased at least threefold. We suggest that this is due primarily to controls at the level of synthesis of messenger ribonucleic acid for ribosomal proteins but may also involve changes in messenger ribonucleic acid stability. In contrast, a nutritional shift-up causes a stimulation of the synthesis of ribosomal proteins. Experiments designed to determine the hierarchy of stimuli affecting the synthesis of these proteins demonstrated that temperature shock was dominant to glucose stimulation. When a culture growing on ethanol was shifted from 23 to 36 degrees C and glucose was added shortly afterward, the decline in ribosomal protein synthesis continued unabated. However, in wild-type cells ribosomal protein synthesis began to recover within 15 min. In mutants temperature sensitive for ribosome synthesis, e.g., rna2, there was no recovery in the synthesis of most ribosomal proteins, suggesting that the product of rna2 is essential for the production of these proteins under all vegetative conditions.

Hierarchy of elements regulating synthesis of ribosomal proteins in Saccharomyces cerevisiae

1981 ◽  
Vol 1 (11) ◽  
pp. 1016-1023
Author(s):  
D R Kief ◽  
J R Warner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Ribonucleic Acid ◽  
Ribosomal Proteins ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Messenger Ribonucleic Acid ◽  
Ribosomal Protein Synthesis ◽  
Stimulation Of

Saccharomyces cerevisiae cells respond to a heat shock by temporarily slowing the synthesis of ribosomal proteins (C. Gorenstein and J. R. Warner, Proc. Natl. Acad. Sci. U.S.A. 73:1574-1551, 1976). When cultures growing oxidatively on ethanol as the sole carbon source were shifted from 23 to 36 degrees C, the synthesis of ribosomal proteins was coordinately inhibited twice as rapidly and 45% more severely than in comparable cultures growing fermentatively on glucose. Within 15 min, the relative rates of synthesis of at least 30 ribosomal proteins declined to less than one-sixth their initial values, whereas the overall rate of protein synthesis increased at least threefold. We suggest that this is due primarily to controls at the level of synthesis of messenger ribonucleic acid for ribosomal proteins but may also involve changes in messenger ribonucleic acid stability. In contrast, a nutritional shift-up causes a stimulation of the synthesis of ribosomal proteins. Experiments designed to determine the hierarchy of stimuli affecting the synthesis of these proteins demonstrated that temperature shock was dominant to glucose stimulation. When a culture growing on ethanol was shifted from 23 to 36 degrees C and glucose was added shortly afterward, the decline in ribosomal protein synthesis continued unabated. However, in wild-type cells ribosomal protein synthesis began to recover within 15 min. In mutants temperature sensitive for ribosome synthesis, e.g., rna2, there was no recovery in the synthesis of most ribosomal proteins, suggesting that the product of rna2 is essential for the production of these proteins under all vegetative conditions.

Translational regulation of ribosomal protein synthesis during xenopus development

1989 ◽  
Vol 27 ◽  
pp. 219
Author(s):  
B. Cardinali ◽  
C. Bagni ◽  
F. Amaldi ◽  
N. Campioni ◽  
P. Mariottini ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Translational Regulation ◽  
Xenopus Development ◽  
Ribosomal Protein Synthesis

scholarly journals Somatic uniparental disomy with a rare EFL1 variant causes Shwachman-Diamond syndrome through dysregulating ribosomal protein synthesis

2018 ◽  
Author(s):  
Sangmoon Lee ◽  
Chang Hoon Shin ◽  
Che Ry Hong ◽  
Jun-Dae Kim ◽  
Ah-Ra Kim ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Rare Variant ◽  
Translational Control ◽  
Uniparental Disomy ◽  
Chromosome 15 ◽  
East Asians ◽  
Shwachman Diamond Syndrome ◽  
Ribosomal Protein Synthesis

We present three unrelated Korean Shwachman-Diamond syndrome (SDS) patients that carry an incomplete but identical homozygous EFL1 p.Thr1069Ala variant due to a bone marrow-specific mosaic uniparental disomy (UPD) in chromosome 15. This rare variant is found in 0.017% of East Asians and is asymptomatic in a heterozygous status, but harbors a hypomorphic effect, leading to 80S assembly of ribosomal protein (RP) transcripts. We propose a novel somatically-induced pathogenesis mechanism and EFL1 dysfunction that eventually leads to aberrant translational control and ribosomopathy.

Regulation of Ribosomal Protein Synthesis in Prokaryotes

2021 ◽  
Vol 55 (1) ◽  
pp. 16-36
Author(s):  
A. O. Mikhaylina ◽  
E. Y. Nikonova ◽  
O. S. Kostareva ◽  
S. V. Tishchenko
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Ribosomal Protein Synthesis
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