[Halogenation of nucleic acids. II. Bromination of yeast ribonucleic acids in dimethylformamide medium].
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Bromine↗
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[Effect of vitamin C and folic acid on the protein and ribonucleic acid metabolism of normal and psoriasic skin. Autoradiographic studies].
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Ascorbic Acid↗
Identification of an actin-like protein and of its messenger ribonucleic acid in Saccharomyces cerevisiae.
We have identified a yeast protein that resembles actins from other eucaryotes in its tight binding to pancreatic deoxyribonuclease I, its copolymerizaton with purified muscle actin, its one-dimensional peptide map, and its apparent polymerization into 7-nm filaments. The yeast actin-like protein yielded a single spot on two-dimensional polyacrylamide gel electrophoresis, suggesting that a single protein species was present. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the actin-like protein had an apparent molecular weight of 45,000 compared with 42,000 for muscle actin. In an attempt to identify the messenger ribonucleic acid coding for the actin-like protein, yeast polyadenylic acid-rich ribonucleic acid was translated in wheat germ and reticulocyte cell-free protein-synthesizing systems. The actin-like protein was identified among the translation products of the reticulocyte system by its tight binding to deoxyribonuclease I, its comigration with the in vivo-synthesized actin-like protein during sodium dodecyl sulfate-polyacrylamide gel electrophoresis, an the similarity of its peptide map to that of the in vivo-synthesized protein. A yeast protein synthesized in the wheat-germ system was also found to bind to deoxyribonuclease I and to copolymerize with muscle actin. However, its apparent molecular weight was about 35,000, suggesting that it was a product either of incomplete translation or of proteolytic cleavage of the actin-like protein.
Actins↗
Hexokinase II activity and messenger ribonucleic acid abundance in adipose tissue and skeletal muscle during pregnancy and lactation in rats.
OBJECTIVE: Our purpose was to investigate the influence of pregnancy and lactation on hexokinase II activity and gene expression in adipose tissue and skeletal muscle of rats. STUDY DESIGN: Intraabdominal adipose tissue and femoral quadriceps muscle were removed from Sprague-Dawley rats at various times (6 to 10 animals per group) during pregnancy and lactation. Hexokinase II messenger ribonucleic acid was assayed by quantitative ribonuclease protection analysis, and hexokinase activity was measured with the glucose-6-phosphate-coupled assay. RESULTS: The amount of hexokinase II messenger ribonucleic acid in adipose tissue on day 20 of pregnancy was 55.4% +/- 8.4% (p < 0.01, unpaired Student t test) of the value for nonpregnant control rats; hexokinase II activity was also decreased in this tissue at this time (39.34 +/- 3.05 vs 27.81 +/- 3.61 mU x min(-1) x mg protein(-1), p < 0.05). Hexokinase II activity and messenger ribonucleic acid abundance in skeletal muscle were unaffected by pregnancy and lactation. CONCLUSION: Both hexokinase II messenger ribonucleic acid abundance and enzyme activity are reduced in adipose tissue of pregnant rats near term, possibly contributing to the insulin resistance associated with late pregnancy.
Adipose Tissue↗
Specialized lambda transducing bacteriophage which carries hisS, the structural gene for histidyl-transfer ribonucleic acid synthetase.
A number of specialized lambda transducing bacteriophages which carry the Escherichia coli gene guaB were isolated from E. coli. One of these bacteriophages, lambda cI857 Sam7 d guaB-2, also carries hisS, the structural gene for histidyl-transfer ribonucleic acid synthetase (EC 6.1.1.21). Histidyl-transfer ribonucleic acid synthetase activities in induced and uninduced lysogens carrying lambda d guaB-2 indicate that the phage carries the entire structural gene and that the gene is under the control of an E. coli promoter. These conclusions were confirmed by the in vivo production of a protein encoded by the phage which comigrates with authentic histidyl-transfer ribonucleic acid synthetase on two-dimensional polyacrylamide gels.
Amino Acyl-tRNA Synthetases↗
Effect of actinomycin D and oxygen on the ribonucleic acid synthesis of an anaerobic gram-negative bacterium.
The synthesis of ribonucleic acid by whole cells of Bacteroides ruminicola is not sensitive to actinomycin D, but it is sensitive to actinomycin D in the presence of ethylenediaminetetraacetate. Ribonucleic acid synthesis by whole cells of this gram-negative anaerobic bacterium is also totally inhibited by oxygen.
Anaerobiosis↗
Non-coding ribonucleic acids--a class of their own?
Non-coding ribonucleic acids (RNAs) do not contain a peptide-encoding open reading frame and are therefore not translated into proteins. They are expressed in all phyla, and in eukaryotic cells they are found in the nucleus, cytoplasm, and mitochondria. Non-coding RNAs either can exert structural functions, as do transfer and ribosomal RNAs, or they can regulate gene expression. Non-coding RNAs with regulatory functions differ in size ranging from a few nucleotides to over 100 kb and have diverse cell- or development-specific functions. Some of the non-coding RNAs associate with human diseases. This chapter summarizes the current knowledge about regulatory non-coding RNAs.
Animals↗
Phenylalanyl-tRNA synthetase of baker's yeast. Modulation of adenosine triphosphate-pyrophosphate exchange by transfer ribonucleic acid.
Native and modified phenylalanine transfer ribonucleic acid (tRNAPhe) can modulate phenylalanine-dependent adenosine triphosphate--inorganic [32P]pyrophosphate (ATP--[32P]PPi) exchange activity via inhibition of adenylate synthesis. Inhibition is visualized if concentrations of L-phenylalanine, ATP, and pyrophosphate are subsaturating. In the proposed mechanism, tRNAPhe is a noncompetitive inhibitor at conditions where only one of the two active sites per molecule of enzyme is occupied by L-phenylalanine, ATP, and pyrophosphate. At saturating concentrations of these reactants, both active sites are occupied and, according to the model, inhibition is eliminated. Occupation by these reactants is assumed to follow homotropic negative cooperativity. The type of effects depends on modification of tRNAPhe. Native tRNAPhe, tRNA2'-dAPhe, and tRNAoxi-redPhe are inhibitors, tRNAPhepCpC has no effect, and tRNAoxPhe is an activator. Kinetics of activation by tRNAoxPhe are slow, following the time course of Schiff base formation and subsequent reduction by added cyanoborohydride. Besides showing that a putative enzyme amino group is nonessential for substrate binding and adenylate synthesis, this result may suggest that an enzyme amino group could interact with the 3'-terminal adenyl group of cognate tRNA. In the case of asymmetrical occupation of the enzyme active sites by all of the small reactants ATP, L-phenylalanine, and pyrophosphate, the interaction with the amino group might trigger the observed noncompetitive inhibition of the pyrophosphate exchange by tRNAPhe.
Adenosine Triphosphate↗
Hormonal control of messenger ribonucleic acid metabolism in barley aleurone layers.
Ribonucleic acid containing poly(adenylic acid) [poly(A)-RNA] is present in barley aleurone layers. This poly(A)-RNA becomes labeled with radioactive precursors of RNA during the incubation of isolated aleurone layers with or without gibberellic acid. However, the rate of synthesis of poly(A)-RNA is enhanced by gibberellic acid. This enhancement begins within 3-4 hr of addition of the hormone and reaches a maximum, which is about 50-60% over the control, 10-12 hr after addition of the hormone. Cordycepin inhibits total RNA as well as poly(A)-RNA synthesis in barley aleurone layers. However, cordycepin inhibits the hormone-controlled synthesis of alpha-amylase (EC 3.2.1.1) only if it is added 12 hr or less after gibberellic acid. The insensitivity of alpha-amylase production to cordycepin after 12 hr of gibberellic acid treatment suggests that alpha-amylase is translated from stable messenger RNA.
Adenine Nucleotides↗
Conformation and recognition control of peptide ribonucleic acid containing pyrimidine/purine mixed sequence.
Peptide ribonucleic acids (PRNA), tethering 5'-amino-5'-deoxyribonucleoside as a recognition moiety for RNA/DNA, have been designed and synthesized, as a novel nucleic acid model. External switching of the recognition behavior of PRNA containing not only pyrimidine nucleobase but also purine nucleobase, with complementary oligomeric DNA/RNA has been demonstrated for the first time through both the orientational switching of the nucleobase of PRNA and electrostatic repulsion between borate ester anion of PRNA and phosphodiester anion of DNA/RNA, induced by added borates.
Base Sequence↗
Interaction of neomycin with ribosomes and ribosomal ribonucleic acid.
Neomycin binds ribosomes and ribosomal ribonucleic acid (rRNA) in vivo and in vitro producing changes detectable by increases in gel electrophoretic mobility. These changes were observed in gels that contain ethylenediaminetetraacetic acid or no added magnesium ion. The progressive increase in gel electrophoretic mobility with increasing antibiotic concentrations suggests that neomycin is binding at multiple sites on RNA. The binding was reversible but sufficiently stable to survive dialysis and electrophoresis. It is proposed that bound neomycin stabilizes the ribosome and RNA structures, restricting the unfolding of the particles during electrophoresis and thus allowing for a more rapid migration in the gel. Gentamicin produced an effect similar to that of neomycin. Paromomycin, differing from neomycin by only one amino group, had considerably less effect on ribosome and rRNA mobilities. The binding of neomycin to rRNA improved the linearity of the plot of log molecular weight versus mobility and thus may be of benefit in providing a more accurate estimation of molecular weights of large RNAs.
Anti-Bacterial Agents↗
Double-stranded ribonucleic acid from Mengo virus: production, characterization, and interferon-inducing and antiviral activities in comparison with polyriboinosinic-polyribocytidylic acid.
Mengo virus double-stranded ribonucleic acid (dsRNA) was obtained on a semi-industrial scale from infected cultures of BHK-21 cells grown in suspension. Yield of the extraction and purification operations was small (about 22 mg from 10(11) cells in a 100-liter culture). Physicochemical characterization of this dsRNA gave an estimated molecular weight close to 4 x 10(6), a density of 1.59 (similar to that of the poliovirus dsRNA), and a thermal transition midpoint of 94 C. This product was a little more toxic for the mouse, by the intravenous route, than polyriboinosinic . polyribocytidylic acid (poly I:C) and strictly comparable in this respect to poliovirus dsRNA. The interferon-inducing capacity in the mouse and the antiviral activities in the mouse (infected with encephalomyocarditis, Semliki Forest, influenza, foot-and-mouth disease, and murine hepatitis viruses) and in the rabbit (Shope fibroma virus) of the ultraviolet light-inactivated product were practically identical, on a quantitative basis, with those of poly I:C. In vitro and in vivo experiments showed the dsRNA from Mengo virus to be slightly but significantly more resistant than poly I:C to the inactivating effect of human serum.
Animals↗
Thermosensitive mutants of Escherichia coli K-12 altered in the catalytic Subunit and in a Regulatory factor of the glutamy-transfer ribonucleic acid synthetase.
The glutamyl-transfer ribonucleic acid synthetase (GluRS) of a partial revertants (ts plus or minus) of the thermosensitive (ts) mutant strain JP1449 (LOcus gltx) and of a ts mutant strain EM111-ts1 with a lesion in or near the locus gltx have been studied to find the relation between these two genetic loci known to influence the GluRS activity in vitro and the presence of a catalytic subunit and of a regulatory subunit in the GluRS purified from Escherichia coli K-12. The ts character of strain JP1449-18ts plus or minus is co-transduced with the marker dsdA at the same frequency as is the ts character of strain JP1449. Its purified GluRS is very thermolabile and its Km for glutamate is higher than that of a wild-type GluRS. These results indicate that the locus gltX is in the structural gene for the catalytic subunit of this enzyme. The location of the mutation causing the partial ts reversion in strain JP1449-18ts plus or minus is discussed. The GluRS purified from the ts mutant strain EM111-ts1 has the same stability as the wild-type enzyme, but its Km forglutamate increases with the temperature, suggesting that the locus gltE codes for a regulatory factor, possibly for the polypeptide chain that is co-purified with the catalytic subunit.
Acylation↗
Properties of polyadenylate-associated ribonucleic acid from Saccharomyces cerevisiae ascospores.
Bulk ribonucleic acid (RNA) was isolated from mechanically disrupted ascospores of Saccharomyces cerevisiae. After two passes over an oligo (dT10) cellulose column, the portion which bound, called poly(A)(+), was characterized. It is heterodisperse in size with a mean molecular weight of approximately 4 X 10(5), but contains some species as large as 7 X 10(5). The base composition is similar to vegetative poly(A)(+) RNA. The polyadenylate segment is also heterogenous in size, ranging from 90 to 20 bases in length, with a peak at approximately 60 nucleotides in length. Pulse-labeling of asci with [3H-methyl]methionine yields two "caps," 7-methyl guanosine-5'-triphosphoryl-5'-adenosine (or guanosine) identical to that found in vegetative poly(A)(+) RNA. The poly(A)(+) RNA in spores is found in polyribosomes which are, on the average, smaller than vegetative ones. Long-term labeling studies indicate that the fraction of poly(A)(+) RNA in spores is similar to that in vegetative cells.
Base Sequence↗
Reovirus-induced ribonucleic acid polymerase.
A virus-induced ribonucleic acid (RNA) polymerase activity was found in L cells infected with type 3 reovirus. Most of the enzyme is associated with the "large particle" fraction of the infected cells. The enzyme first appeared at 3 to 5 hr after infection and increased in amount until 7 to 9 hr. All four ribonucleoside triphosphates are incorporated in vitro into an acid-insoluble form by the enzyme. The major part of the product formed in vitro is a double-stranded RNA indistinguishable from viral RNA by electrophoresis on polyacrylamide gel. Approximately 40% of the product is a single-stranded RNA of relatively small molecular weight. More than 95% of the nucleotides incorporated into double-stranded RNA by the enzyme are bound in internal 3'-5'-phosphodiester linkages extending back from both 3'- and 5'-termini of the RNA strands.
Acrylates↗
Electron microscopic observations on the ribonucleic acid of murine leukemia virus.
The ribonucleic acid (RNA) of murine leukemia virus (MLV) Rauscher strain was observed by the aid of electron microscopy with the use of the protein monolayer technique. RNA was observed directly after release from virus particles or after isolation by sedimentation in sucrose density gradients. Molecules were found in an extended linear form. Many of the RNA filaments released by detergent treatment contained curled regions, suggesting the linear filaments were originally coiled within the virus particle. The relationship of the curled areas to the containment of the RNA within the virus particle is discussed, and a mechanism for the inclusion of RNA in the budding virion is proposed. Treatment of the extended MLV-RNA with dimethyl sulfoxide resulted in the collapse of the molecule forming a tangled complex. Treatment with urea or heating at 50 C in 3 mm NaCl also produced this effect. Also under the conditions in which MLV-RNA was linear, RNA from Rous sarcoma virus also was linear, but Newcastle disease virus RNA and ribosomal RNA of rat liver had collapsed structures. The results indicated that the RNA of MLV, and perhaps other RNA-containing tumor viruses, has a specific unique conformation dependent upon hydrogen bonds.
Avian Sarcoma Viruses↗
Mumps virus replication in chick embryo lung cells: properties of ribonucleic acids in virions and infected cells.
Ribonucleic acid (RNA) species in mumps virions and in infected cells were compared. The predominant RNA species in virions labeled with (3)H-uridine sedimented at 50S; RNA species sedimenting at 28, 18, and about 10S were also present. The virion-associated RNA species sedimenting slower than 50S contained some nucleotide sequences similar to 50S virion RNA. Although mumps virus replication was severely inhibited by high concentrations of actinomycin D, some virus was made, and virus-specific RNA species accumulated in infected cells. Mumps virus resembled other paramyxoviruses in inducing, in infected cells, synthesis not only of 50S RNA but also of slower sedimenting RNA species with a peak distribution at about 18S, complementary in base sequences to 50S virion RNA. In addition, base sequences of the parental type were relatively abundant in the RNA species sedimenting slower than 50S; these may represent precursors of the slowly sedimenting RNA species associated with virions. Ribonuclease-resistant RNA was detected in infected cells; this may represent replicative or transcriptive intermediates. Inhibition of protein synthesis with cycloheximide severely depressed accumulation of labeled 50S RNA in infected cells but did not interfere with accumulation of RNA species sedimenting slower than 50S. Actinomycin D treatment had a similar effect. Annealing of genomes and virus-induced complementary RNA species of Newcastle disease virus, Sendai virus, and mumps virus did not reveal any base sequence homologies.
Animals↗
Fetal esophageal ligation induces expression of vascular endothelial growth factor messenger ribonucleic acid in fetal membranes.
OBJECTIVE: Obstruction of the fetal esophagus does not always produce the expected polyhydramnios. This is because of increased intramembranous absorption of amniotic fluid into the fetal circulation. A possible mediator for this increased absorption is vascular endothelial growth factor (VEGF). The present objective was to explore whether VEGF gene expression and action would be induced in fetal membranes and placentas of ovine fetuses after esophageal ligation. STUDY DESIGN: Five late-gestation fetal sheep underwent esophageal ligation and 5 served as control animals. On postoperative day 9, amnion, chorion, and placenta were collected for cellular localization and quantitation of VEGF messenger ribonucleic acid by in situ hybridization and Northern blot analysis. Reverse-transcription polymerase chain reaction was used to identify the VEGF molecular forms. Immunostaining with Ki-67 antibody was used to determine the proliferation of vascular endothelium in the fetal membranes and placentas. RESULTS: VEGF messenger ribonucleic acid was localized in amniotic epithelium, chorionic cytotrophoblast, and cytotrophoblast of the placenta. VEGF164 was the major transcript expressed in these tissues. The abundance of VEGF messenger ribonucleic acid in the amnion and chorion, but not in the placenta, was significantly increased in the ligated fetuses in comparison with the control fetuses. The proliferation of the intramembranous blood vessel endothelium was greater in the ligated fetuses than in the control fetuses. CONCLUSION: The levels of VEGF messenger ribonucleic acid and the proliferation of vascular endothelium in the amnion and chorion increased after fetal esophageal ligation. This provides a possible mechanism for the enhanced intramembranous absorption of amniotic fluid through increased vascularity and permeability of the fetal membranes, thus ameliorating the development of polyhydramnios. We speculate that the signal(s) that mediate the increase in VEGF expression is present in either the fetal urine or the fetal lung secretions, or both.
Amnion↗