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At least 1,063 records · Page 59Linked to original sources
PubMed1969

A new approach to the analysis of hybridization of bacterial nucleic acids. Analysis of the ribosomal ribonucleic acids of Bacillus subtilis.

A new graphical analytical technique is described for the hybridization of bacterial RNA with denatured homologous DNA immobilized on cellulose nitrate membrane filters. To a constant amount of DNA, various amounts of bacterial RNA were added and the percentage of input RNA bound was plotted against the DNA/RNA weight ratio in a given experiment. When RNA samples were used that hybridize to denatured DNA as a single species, the resulting curves (RNA-hybridization-efficiency curves) could be analysed to show the percentage of the DNA capable of specifically binding the RNA and could also be used to detect the presence of minor RNA contaminants in a purified specimen. The method could also estimate the relative amounts of two species of RNA in a mixture when these were hybridized independently to different DNA cistrons or cistron groups. As an example of RNA that can be studied in this way, the 16s and 23s ribosomal RNA species of Bacillus subtilis were chosen. These each behave in DNA-RNA hybridization as a single species and bind independently to different groups of DNA cistrons. The results obtained from hybridization-efficiency curves were compared with those obtained by the more usual method of saturating the specific DNA regions with excess of ribosomal RNA (hybridization-saturation curves). It was confirmed by both approaches that 0.15 (+/-0.02)% of B. subtilis DNA would hybridize with 16s ribosomal RNA, 0.30 (+/-0.02)% would hybridize with 23s ribosomal RNA, and 0.46 (+/-0.02)% would hybridize with (16s+23s) ribosomal RNA. This agreement suggested that mass-action equilibria between hybridized and free RNA had a negligible effect on the hybridization curves over the range of DNA and RNA concentrations employed.

Bacillus subtilis↗
PubMed1970

Possible inhibitory effect of teichoic acid on Bacillus subtilis transfer ribonucleic acid.

1. tRNA of Bacillus subtilis was found to be variably contaminated with membrane teichoic acid. 2. Samples with high contents of teichoic acid showed no accepting activity for tRNA(Phe) and tRNA(Tyr). 3. Removal of teichoic acid restored accepting activity and fractions containing teichoic acid, separated on Sephadex G-150, inhibited the charging of tRNA(Tyr). 4. The presence of teichoic acid did not inhibit the charging of tRNA(His).

Bacillus subtilis↗
PubMed1971

Amino acid regulation of synthesis of ribonucleic acid and protein in the liver of rats.

Weanling (23-day-old) rats were fed on either a low-protein diet (6% casein) or a diet containing an adequate amount of protein (18% casein) for 28 days. Hepatic cells from animals fed on the deficient diet were characterized by markedly lower concentrations of protein and RNA in all cellular fractions as compared with cells from control rats. The bound rRNA fraction was decreased to the greatest degree, whereas the free ribosomal concentrations were only slightly less than in control animals. A good correlation was observed between the rate of hepatic protein synthesis in vivo and the cellular protein content of the liver. Rates of protein synthesis both in vivo and in vitro were directly correlated with the hepatic concentration of individual free amino acids that are essential for protein synthesis. The decreased protein-synthetic ability of the ribosomes from the liver of protein-deprived rats was related to a decrease in the number of active ribosomes and heavy polyribosomes. The lower ribosomal content of the hepatocytes was correlated with the decreased concentration of essential free amino acids. In the protein-deprived rats, the rate of accumulation of newly synthesized cytoplasmic rRNA was markedly decreased compared with control animals. From these results it was concluded that amino acids regulate protein synthesis (1) by affecting the number of ribosomes that actively synthesize protein and (2) by inhibiting the rate of synthesis of new ribosomes. Both of these processes may involve the synthesis of proteins with a rapid rate of turnover.

Amino Acids↗
PubMed1973

Interaction between polyuridylic acid and rabbit globin messenger ribonucleic acid.

Poly(U) binds to globin mRNA in 0.1m-NaCl. Studies with ribonuclease digestion of this complex suggest that there are polyadenylate-rich sequences in the mRNA containing about 30-40 adenylate residues. The sequences appear to be homogenous and of approximately the same length for both alpha- and beta-globin mRNA. They are most likely located at the 3' terminus of the molecule.

Animals↗
PubMed2003

A novel strategy for reversible control of conformation and DNA/RNA recognition of peptide ribonucleic acid (PRNA) by external factors.

A novel nucleic acid model using peptide ribonucleic acid (PRNA), which contains 5'-amino-5'-deoxyribonucleoside as a recognition site for nucleic acids, has been designed, synthesized and applied to the external reversible control of recognition behavior of the complementary oligomeric DNA through the orientational switching of the nucleobase induced by borates. In case of PRNA 12-mers, efficient orientational change of nucleobases was observed. Furthermore, these oligomeric PRNAs form a stable complex with complementary DNA's and the recognition behavior of oligomeric PRNAs with DNA's is controlled by the borate added as an external factor.

DNA↗
PubMed2000

Synthesis and conformation control of peptide ribonucleic acid containing 5'-amino-5'-deoxyribopurinenucleosides.

A novel nucleic acid model, i.e. peptide ribonucleic acid (PRNA), tethering 5'-amino-5'-deoxypyrimidine ribonucleoside as a recognition site for nucleic acids, has been designed and synthesized. We have demonstrated that the recognition behavior of PRNA with complementary oligopurinenucleotides can be controlled externally through the orientational switching of the pyrimidine nucleobase of PRNA induced by added borates. We extend this methodology of controlling the nucleobase orientation and recognition behavior of novel mono and oligomeric PRNAs containing 5'-amino-5'-deoxypyrimidine and/or purinenucleosides. In case of the PRNA oligomer containing pyrimidine-purine mixed sequence, efficient orientational switching of nucleobases induced by added borates was also observed.

Borates↗
PubMed2004

Synthesis of peptide ribonucleic acid consisting of D- and L-gamma-glutamic acid as a backbone structure.

A novel nucleic acid model using peptide ribonucleic acid (PRNA), which contains 5-amino-5-deoxyribonucleoside as a recognition site for nucleic acids and consists D-glutamic acid (D-PRNA) instead of L-glutamic acid (L-PRNA) as a backbone structure, has been designed and synthesized. Difference between D-PRNA and L-PRNA oligomers was elucidated on the basis of the effects of chirality of gamma-glutamic acid backbone upon structure elucidated by CD spectra.

Buffers↗
PubMed1975

The interaction of fusidic acid with peptidyl-transfer-ribonucleic-acid - ribosome complexes.

The inhibitory action of fusidic acid on peptide-chain elongation was studied with systems in vitro directed by either polyuridylic acid or endogenous messenger (Escherichia coli polysomes washed with 1 M NH4Cl) or R17 RNA, and supplemented with either crude or purified elongation factors. In all cases strong inhibition of synthesis required high concentrations of the antibiotic (approx. 1 mM), while a similar inhibition of the EF-G-plus-ribosome-dependent GTP hydrolysis required between 10 and 100 times less antibiotic. Since most of the GTP hydrolysis observed was presumably due to free ribosomes (without aminoacyl-tRNA or peptidyl-tRNA), fusidic acid seemed to interact far more easily with these ribosomes than with ribosomes engaged in peptide-chain elongation. The role of the GDP-EF-G-ribosome-fusidic acid complex in the inhibition of polypeptide synthesis was assessed by measuring formation of this complex on polysomes engaged in peptide-chain elongation. Using purified elongation factors the complex formed on only 25-35% of ribosomes, as measured either by retention of [3H]GDP or by hydrolysis of [3H, gamma-32P]GTP. In contrast, with crude factors (S 100 extract) it formed on more than 70% of ribosomes. The results are compatible with the postulated role of the complex in polypeptide synthesis inhibition (blockade of the ribosomal acceptor site and subsequent inhibition of aminoacyl-tRNA binding) and indicate that formation of the complex takes place by overriding the control that prevents interaction of EF-G when the donor site is occupied by peptidyl-tRNA. In the polyuridylic-acid-directed system for synthesis of oligophenylalanine the antibiotic inhibits every round of peptide elongation, including dipeptide formation, to roughly the same extent.

Binding Sites↗