scholarly journals Studies on the 3′-terminal sequences of the large ribosomal ribonucleic acid of different eukaryotes and those associated with ‘hidden’ breaks in heat-dissociable insect 26S ribonucleic acid

1974 ◽  
Vol 141 (3) ◽  
pp. 617-625 ◽  
Author(s):  
John Shine ◽  
John A. Hunt ◽  
Lynn Dalgarno
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Drosophila Melanogaster ◽  
Ribonucleic Acid ◽  
Galleria Mellonella ◽  
Terminal Sequence ◽  
6S Rna ◽  
Ribosomal Ribonucleic Acid ◽  
Higher Eukaryotes ◽  
26S Rrna ◽  
Polynucleotide Chain

The 3′-terminal sequences associated with the large rRNA complex from a range of eukaryotes were determined after pancreatic or T1-ribonuclease digestion of RNA terminally labelled with [3H]isoniazid. In all higher eukaryotes examined except Drosophila melanogaster, the 3′-terminal sequences Y-G-UOH and G-C-UOH were demonstrated for the large RNA component(s) and for 6S RNA respectively. The 3′-terminal sequence of Saccharomyces cerevisiae 26S RNA was Y-G-UOH and that of 6S RNA Y-A-U-U-UOH. Three 3′-terminal sequences were found in equimolar amounts in the heat-dissociable 26S rRNA characteristic of insect ribosomes. These were Y-G-U-G-UOH, Y-C-G-UOH and G-C-UOH for cultured Antheraea eucalypti cells, Y-G-UOH, Y-G-UOH and G-C-UOH for Galleria mellonella larvae and Y-C-G-AOH, Y-G-U-AOH and G-Y-U-GOH for Drosophila melanogaster flies. Thus the introduction of the central scission in insect 26S rRNA results in the generation of a unique 3′-terminus and does not arise from random cleavage of the polynucleotide chain.

scholarly journals Identical 3′-terminal octanucleotide sequence in 18S ribosomal ribonucleic acid from different eukaryotes. A proposed role for this sequence in the recognition of terminator codons

1974 ◽  
Vol 141 (3) ◽  
pp. 609-615 ◽  
Author(s):  
John Shine ◽  
Lynn Dalgarno
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Synthesis ◽  
Drosophila Melanogaster ◽  
Ribosomal Rna ◽  
Ribonucleic Acid ◽  
18S Rrna ◽  
Base Sequence ◽  
Terminal Sequence ◽  
Ribosomal Ribonucleic Acid ◽  
Rrna Species

The 3′-terminal sequence of 18S ribosomal RNA from Drosophila melanogaster and Saccharomyces cerevisiae was determined by stepwise degradation from the 3′-terminus and labelling with [3H]isoniazid. The sequence G-A-U-C-A-U-U-AOH was found at the 3′-terminus of both 18S rRNA species. Less extensive data for 18S RNA from a number of other eukaryotes are consistent with the same 3′-terminal sequence, and an identical sequence has previously been reported for the 3′-end of rabbit reticulocyte 18S rRNA (Hunt, 1970). These results suggest that the base sequence in this region is strongly conserved and may be identical in all eukaryotes. As the 3′-terminal hexanucleotide is complementary to eukaryotic terminator codons we discuss the possibility that the 3′-end of 18S rRNA may have a direct base-pairing role in the termination of protein synthesis.

scholarly journals Molecular integrity of chloroplast ribosomal ribonucleic acid

1973 ◽  
Vol 135 (1) ◽  
pp. 237-240 ◽  
Author(s):  
Christopher J. Leaver
Keyword(s):  
Secondary Structure ◽  
Hydrogen Bonds ◽  
Ribonucleic Acid ◽  
Low Temperatures ◽  
Ribosomal Ribonucleic Acid ◽  
Polynucleotide Chain

The majority of chloroplast 1.1X106-mol.wt. rRNA molecules are nicked at specific points in the polynucleotide chain, the molecules being kept intact at low temperatures by their secondary structure. Conditions that break hydrogen bonds and lead to loss of secondary structure cause dissociation of the molecule.

scholarly journals Das Ribonukleinsäure-Ribonuklease-System von Saccharomyces cerevisiae: Zur Stoffwechselregulation bei Eukaryoten / On the Metabolic Regulation in Eucaryotes: The Ribonucleic Acid-Ribonuclease System in Saccharomyces cerevisiae

1971 ◽  
Vol 26 (4) ◽  
pp. 328-336 ◽  
Author(s):  
Gerhard F. Stärk ◽  
Lothar Jaenicke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribonucleic Acid ◽  
Metabolic Regulation ◽  
Specific Growth ◽  
Growth Conditions ◽  
Mitochondrial Enzymes ◽  
Respiratory Enzymes ◽  
Growing Cell ◽  
Ribosomal Ribonucleic Acid ◽  
Logarithmic Growth

A “latent” ribosomal ribonuclease was demonstrated in Saccharomyces cerevisiae which was repressed by glucose parallel to the respiratory enzymes during logarithmic growth. It was induced by oxygen after consumption of glucose, and while the cells were growing on ethanol. In the growing cell, this ribonuclease was associated with the ribosomes. It hydrolyzed non-functional polynucleotide bonds only leaving untouched the integrity and functionality of the ribosomal structure. Though this ribonuclease was not integrated into the mitochondria, its synthesis depended upon the intact and coupled respiratory chain, similar to the mitochondrial enzymes proper. The function of the ribosomal ribonuclease seems to be the adaptation of the ribosomal ribonucleic acid content to the specific growth conditions together with the protein synthesis capacity of the cell. Hence, the enzyme serves the economy of the cell: when the cells grow fast during the fermentative phase only little ribonucleic acid is degraded; during the oxidative phase, when metabolic activity is low, ribonucleic acid is hydrolzyed as a saving mechanism. The switching between glycolytic and aerobic metabolism, which is brought about by alternating synthesis of the respective enzymes, is closely related to the ribonucleic acid turnover in the yeast cell and is probably regulated analogously in higher organisms.

scholarly journals Spectroscopic evidence for the uneven distribution of adenine and uracil residues in ribosomal ribonucleic acid of Drosophila melanogaster and of Plasmodium knowlesi and its possible evolutionary significance

1976 ◽  
Vol 155 (3) ◽  
pp. 465-475 ◽  
Author(s):  
R A Cox ◽  
E Godwin ◽  
J R Hastings
Keyword(s):  
Drosophila Melanogaster ◽  
Plasmodium Knowlesi ◽  
Nucleotide Composition ◽  
Evolutionary Significance ◽  
Base Pairs ◽  
Parasite Plasmodium ◽  
Ribosomal Ribonucleic Acid ◽  
Principal Species ◽  
Polynucleotide Chain ◽  
Hypochromic Effect

RNA was isolated from subribosomal particles of the malaria parasite Plasmodium knowlesi. The nucleotide composition (mole fraction) of the principal species was obtained (S-rRNA, 0.295A, 0.36U, 0.25G, 0.105C: L-rRNA, 0.326A, 0.31U, 0.228G, 0.144C). Ribosomal RNA was also isolated from Drosophila melanogaster. Optical properties of these A + U-rich species were measured. In all four cases analysis of the hypochromic effect revealed that adenine and uracil residues tended to form clusters along the polynucleotide chain. A substantial fraction of residues was located in bihelical regions of approx. 50% G-C base pairs or in regions of approx. 30-35% G-C base pairs. The possible evolutionary significance of these results was considered on the basis of comparison with properties of rRNA from bacteria (Escherichia coli) and a mammal (rabbit reticulocyte).

scholarly journals Coordinate control of syntheses of ribosomal ribonucleic acid and ribosomal proteins during nutritional shift-up in Saccharomyces cerevisiae.

1981 ◽  
Vol 1 (11) ◽  
pp. 1007-1015 ◽  
Author(s):  
D R Kief ◽  
J R Warner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Steady State ◽  
Ribonucleic Acid ◽  
Ribosomal Proteins ◽  
Acid Synthesis ◽  
State Characteristic ◽  
Coordinate Control ◽  
Ribosomal Ribonucleic Acid ◽  
Ribosomal Precursor ◽  
Stimulation Of

We investigated the regulation of ribosome synthesis in Saccharomyces cerevisiae growing at different rates and in response to a growth stimulus. The ribosome content and the rates of synthesis of ribosomal ribonucleic acid and of ribosomal proteins were compared in cultures growing in minimal medium with either glucose or ethanol as a carbon source. The results demonstrated that ribosome content is proportional to growth rate. Moreover, these steady-state concentrations are regulated at the level of synthesis of ribosomal precursor ribonucleic acid and of ribosomal proteins. When cultures growing on ethanol were enriched with glucose, the rate of ribosomal ribonucleic acid synthesis, measured by pulsing cells with [methyl-3H]methionine, increased by 40% within 5 min, doubled within 15 min, and reached a steady state characteristic of the new growth medium by 30 min. Labeling with [3H]leucine reveal a coordinate increase in the rate of synthesis of 30 or more ribosomal proteins as compared with that of total cellular proteins. Their synthesis was stimulated approximately 2.5-fold within 15 min and nearly 4-fold within 60 min. The data suggest that S. cerevisiae responds to a growth stimulus by preferential stimulation of the synthesis of ribosomal ribonucleic acid and ribosomal proteins.

Small Ribosomal Ribonucleic Acid Species of Saccharomyces cerevisiae

1971 ◽  
Vol 105 (1) ◽  
pp. 101-106 ◽  
Author(s):  
Stephen A. Udem ◽  
Karen Kaufman ◽  
Jonathan R. Warner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribonucleic Acid ◽  
Ribosomal Ribonucleic Acid
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