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PubMed1976

Effects of some polynucleotides on DNA synthesis in human lymphocytes.

The effect of several single-and double-stranded synthetic polyribonucleotides on the 3H-thymidine incorporation in intact and PHA-stimulated human lymphocyte cultures was investigated. Only polyuridilic and polyguanilic acids were found to stimulate DNA synthesis in the intact cells. All other polynucleotides tested had much weaker or had no stimulating activity. PHA-activated lymphocytes responded to addition of polynucleotides by the decrease of 3H-thymidine uptake. The mostly profound inhibition of lymphocyte response to PHA was observed with polyguanilic acid.

Adjuvants, Immunologic↗

PubMed1978

Identification of an Escherichia coli nuclease acting on structurally altered transfer RNA molecules.

A nuclease (RNase D) that can recognize structurally altered transfer RNA molecules has been partially purified from Escherichia coli. The enzyme acts poorly on intact tRNA and is inactive with the synthetic polyribonucleotides, poly(A), poly(U), or double-stranded poly(A).poly(U). The enzyme requires Mg2+ for activity and is stimulated by the monovalent cations, K+ and NH4+. The products of the reaction are 5'-mononucleotides. The molecular weight of the protein is about 60,000 as judged by Sephadex G-100 chromatography. The enzyme does not correspond to any known E. coli ribonuclease and may represent an intracellular scavenging mechanism for denatured tRNAs and other inactive RNA molecules.

Cations↗

PubMed1986

Yeast mitochondrial RNA polymerase. Purification and properties of the catalytic subunit.

An RNA polymerase was purified 6500-fold to near homogeneity from a whole cell extract of Saccharomyces cerevisiae. The purified enzyme consists of a single 145,000-dalton polypeptide. By subcellular fractionation, the enzyme was localized to the mitochondria. The RNA polymerase activity is alpha-amanitin- and rifampicin-resistant. With single-stranded DNA templates, the enzyme catalyzes the synthesis of polyribonucleotide chains with lengths ranging from less than 10 to greater than 100 residues. It is inactive with double-stranded DNA. Specific antisera inhibit the RNA polymerase activity and recognize the 145,000-dalton polypeptide. The antisera relate this enzyme to previously described yeast mitochondrial RNA polymerase preparations capable of initiation of transcription at mitochondrial promoter sequences (Winkley, C. S., Keller, M. J., and Jaehning, J. A. (1985) J. Biol. Chem. 260, 14214-14223). It therefore appears that the enzyme is a subunit of the yeast mitochondrial RNA polymerase.

Adenosine Triphosphate↗

PubMed1977

Studies on the chemical composition and biological properties of transfer factor.

Dialyzable transfer factor (dTF) was fractionated on Sephadex G-10 and G-25 fine columns, and biological activity was found in 3 fractions. One of these, designated VIa, and having a tendency to adsorb to the Sephadex G-10 gel, was shown to have a therapeutic effect on certain immunological diseases. Analysis of this fraction on thin-layer and gas chromatography and with infrared and mass spectroscopy indicated that about half of this fraction was composed of uracil; additional unidentified heterocyclic and aromatic substances were present in this fraction. Adjacent fraction V contained tyrosine and a small polyribonucleotide, and fraction VII hypoxanthine and additional unidentified components. Our results suggest that the therapeutic activity of dTF is not mediated through an immunologically specific informational molecule, but is rather based on non-specific stimulation of the expression of the immune response.

Heterocyclic Compounds↗

PubMedDate not supplied

Immunological recognition of three polynucleotide structures associating adenylic and uridylic acids.

The reactions of antibodies directed against the two double-stranded synthetic polyribonucleotide complexes poly(A).poly(U) or poly(I). poly(C) with three polynucleotide structures associating equimolar amounts of adenylic and uridylic acids were studied by immunodiffusion, quantitative precipitation and readioimmunoassay. The three sequence isomers of the same base composition but different nucleotide distribution were: the double helical complex poly(A).poly(U) containing two homopolymeric strands; the copolynucleotide poly(A-U) composed of a strictly repeating riboadenylic acid and ribouridylic acid sequence in both strands; and the copolymer poly(A,U) where the two strands contain both residues but in a random distribution. The three antigens reacted with anti-poly(A).poly(U) and antipoly(I).poly(C) antisera but not to the same extent. The random copolymer poly(A,U) reacted poorly with sera of both specificity. In contrast the reactivity of the alternating copolnucleotide poly(A-U) was widely different according to the specificity of the sera used. Whereas it was recognized by the anti-poly(A).poly(U) antibodies almost to the same extent than the homologous complex, its activity was much lower with anti-poly(I).poly(C) antisera. In addition, the relative efficiency of poly(A-U) was approximately 50 times lower than that of poly(A).poly(U) when tested with anti-poly(I).poly(C) antibody, thereby indicating recognition of different antigenic determinants in both duplexes. Antibodies directed against defined conformational determinants are therefore able to distinguish between three polynucleotide structures of the same base composition but different sequence.

Animals↗

PubMed1980

Nascent RNA chain termination and ultrastructural changes in nucleoli isolated from SV40-transformed fibroblasts treated with aminonucleoside of puromycin.

The mechanism for the selective inhibition of preribosomal RNA synthesis by puromycin aminonucleoside (AMS) was investigated in cultured AG 2804 cells, which are human embryonic lung fibroblasts transformed by SV40 virus. Sequential high voltage electrophoresis and paper chromatography of the RNA of fractionated nuclei isolated from fibroblasts exposed to tritiated AMS (340 microM, 5 microCi. per ml., for 18 hours) demonstrated that the inhibitor is demethylated to 3'-amino-3'-deoxyadenosine and incorporated into terminal positions in both nucleolar and nonnucleolar nuclear RNA chains in the same relative amounts. 3'-Amino-3'-deoxyadenosine was not detected in the RNA obtained from the cytoplasm of AMS-treated fibroblasts. Electron microscopic observation of isolated nucleoli showed that neighboring intranucleolar fibrils have a tendency to coalesce after AMS treatment. It is suggested that, when the modified AMS molecule has reached the growing ends of nascent polyribonucleotide chains elongation stops, the chain remains attached to its template, and the strong positive charge of the aminosugar portion of AMS interacts with negatively charged components (e.g., phosphate groups) of adjacent nascent RNA chains. The high density of the components of the nucleolus produces frequent interactions of this type and leads to secondary interference with nucleolar RNA synthesis, thus accounting for the selective effect of AMS on preribosomal RNA synthesis.

Cell Nucleolus↗

PubMed1983

Inhibition of DNA-dependent RNA polymerase from Escherichia coli by pyran copolymer.

Pyran copolymer, a potent inhibitor of DNA-dependent RNA polymerase from Escherichia coli, prevented polyribonucleotide synthesis by blocking both the initiation and elongation steps. The inhibition was noncompetitive with respect to template and nucleotide triphosphate substrates. Template binding and the stability of the nascent RNA chain were not affected by the inhibitor.

DNA-Directed RNA Polymerases↗

PubMed1978

[Antiviral activity of the complexes obtained at different ratios of complementary homopolyribonucleotides].

Antiviral activity of the complexes of synthetic polyribonucleotides, i.e. poly (I).poly (C) and poly (G).poly (C) obtained at non-equimolar ratios of homopolymers was studied. The system of chick embryon fibroblasts and horse Venezuellan eguine encephalitis virus served as the model. It was shown that the active and stable complexes poly (I).poly (C) and poly (G).poly (C) were formed at some excess of poly (C), i.e. at the ratio of poly G) or poly (I) to poly (C) equal to 40/60 to 20/80 molar per cent. The role of the excessive poly (C) in formation of the stable secondary structure of the nucleotide complexes and its significance as one of the means for affecting the fine structure of double-stranded RNA were discussed.

Animals↗

PubMedDate not supplied

[Induction of plant resistance to the tobacco mosaic virus with a double-stranded poly(G)-poly(C) complex].

Inoculation of double-stranded polyribonucleotide poly(G) . poly(C) complex in a concentration of 50-200 micrograms/mg into tobacco and thornapple leaves was found to produce resistance of the plants to subsequent infection with tobacco mosaic virus (TMV) manifested in decreased number and size of local virus lesions. The induced resistance may spread over the plant and be found in the upper untreated leaves. The level of systemic resistance, however, is much lower than that of the resistance demonstrated in the injected leaves. Actinomycin D (5 micrograms/ml) had no significant effect on the number but stimulated the growth of lesions developing in leaves injected with poly(G) . poly(C) as well as increased their number in the upper leaves of the same plants proximal to the treated ones. Development of tobacco resistance to TMV was accompanied by changes in the activity of terminal oxidases, particularly peroxidase. Possible mechanisms of formation of induced resistance are discussed.

Plant Diseases↗

PubMedDate not supplied

[Nucleotide composition of RNA, synthesized by polynucleotide phosphorylase, in toluene-treated cells of Escherichia coli].

On incubation of cells of E. coli B and MRE 600 (logariphmic phase of growth), treated with toluene in presence of a mixture 14C-nucleoside-5'-diphosphates, Mg2+ or Mn2+ and tris HCl buffer pH 8.0, intracellular synthesis of heteropolyribonucleotide was observed. The synthesis was catalyzed by polynucleotide phosphorylase (PNPase, E. C. 2.7.7.8). An increase in GDP concentration in the medium distinctly decreased the incorporation of other NDP into the polymer (poly-AGUC). If the ratio of ADP, UDP, CDP, GDP in the medium was 1:1:1:0.2, the composition of nitrogenous bases in the heteropolymer produced reflected completely the NDP concentrations in the incubation mixture. Addition of different amino acids (1-lysine, 1-histidine, glycine, 1-phenylalanine) and their mixtures stimulated poly-AGUC synthesis markedly and caused an appreciable alteration in the nucleotide composition of the poly-AGUC synthesized. This phenomenon resembled the effect of amino acids on the activity of partially purified PNPase and on RNA synthesis, catalized by the enzyme in vitro. These data suggest that in bacterial cell, i. e. in vivo, PNPase synthesizes specific RNA polyribonucleotide sequences, participating in protein synthesis or in its regulation.

Amino Acids↗

PubMed1976

Alkaline ribonuclease from rye germ cytosol.

1. Alkaline ribonuclease (pH optimum 7.6) was isolated from rye (Secale cereale L) germ cytosol and partially purified; the preparation was devoid of other nucleolytic activities. 2. The enzyme is a typical endonuclease hydrolysing all phosphodiester bonds in RNA, yielding ultimately purine and pyrimidine nucleoside 2',3'-cyclic phosphates and the corresponding 3'-phosphates. Upon extensive digestion of synthetic polyribonucleotides, pyrimidine, but not purine, nucleoside 3'-phosphates are formed. The enzyme does not hydrolyse synthetic purine cyclic nucleotides. 3. The enzyme does not depolymerize double-stranded complexes of poly(A) and poly(U). 4. Susceptibility to photooxidation and inhibition by 2-hydroxy-5-nitrobenzyl bromide and N-bromosuccinimide implies the involvement of tryptophan residue in the active centre of the enzyme.

Binding Sites↗

PubMed1996

A vibrational spectroscopic study of the metastable form of associated polyinosinic acid.

We have studied by Raman and ir spectroscopy the metastable complex formed by the self-association of polyinosinic acid in aqueous solution. The complex is easily prepared by quickly cooling to ca. 0 degrees C a warm solution of the polyribonucleotide to which a small amount of rubidium salt has been added. Upon heating, this metastable form melts cooperatively near 13 degrees C, well below the dissociation temperature of a stable four-stranded complex, which occurs at 47 degrees C in the same conditions. The presence of several components in the stretching-mode region of the carbonyl groups in the vibrational spectra of the metastable complex suggests that it also has a parallel four-stranded structure. The difference in structure between the two forms is believed to be caused by the presence of fewer metal ions in the central channel of the metastable complex, in agreement with conclusions reached in previous investigations. The Raman spectra further show that the ribose units in the metastable form have a C3'-endo conformation, in contrast with the stable form, for which we have previously suggested a mixed C2'-endo/C3'-endo conformation.

Drug Stability↗

PubMed1994

A vibrational spectroscopic study of the self-association of polyinosinic acid and polyguanylic acid in aqueous solution.

We have studied by Raman and ir spectroscopy the structure of self-associated polyinosinic acid and polyguanylic acid in aqueous solution. The results are consistent with the formation of a four-stranded complex, which melts cooperatively near 60 degrees C in the case of poly(I) in the presence of K+ ions. The conformation of the ribose in both systems is mixed C2'-endo/C3'-endo, giving a structure that is intermediate between the extremes proposed previously from x-ray diffraction studies. Characteristic Raman bands for the C2'-endo ribose conformation in polyribonucleotides are identified. The four-stranded structure of poly(I) appears to be very flexible, with approximately 15% of the tetrameric segments being disrupted and approximately 30% of the ribose units adopting a disordered conformation prior to melting. This disordering process increases to approximately 75% above the melting transition, with the remaining approximately 25% of the ribose units keeping an ordered C2'-endo or C3'-endo conformation.

Nucleic Acid Conformation↗

PubMed1992

Nutrition and malignant disease: implications for surgical practice.

Malignant disease is often associated with weight loss and malnutrition. Nutritional support is frequently provided to patients with cancer in an attempt to improve nutritional status and reverse weight loss, with the aim of reducing morbidity and mortality rates. This review evaluates the effect of supplemental nutrition on morbidity and mortality in patients with malignancy undergoing treatment with surgery, chemotherapy or radiotherapy. It also assesses the effect nutritional supplementation has on host defence mechanisms and how nutrients affect tumour cell growth. The evidence suggests that perioperative nutritional support, if given for at least 10 days, reduces morbidity and mortality in patients with biochemical evidence of severe malnutrition, manifest as a low serum albumin concentration and excessive weight loss. In contrast, there is no evidence that parenteral nutritional support benefits patients undergoing chemotherapy or radiotherapy, in terms of either an increased tumour response rate or prolongation of survival. Current research on malignant disease is highlighting the role of specific nutrients (amino acids, essential fatty acids and polyribonucleotides) as key regulators of both anticancer host defence mechanisms and the control of nitrogen metabolism and tumour growth. Arginine, essential fatty acids and ribonucleotides have all been demonstrated to stimulate antitumour host defence mechanisms and some also modulate tumour cell metabolism. Dietary manipulation offers exciting possibilities for the innovative management of malignant disease.

Adult↗

PubMed1987

A new target for CRP action at the malT promoter.

In Escherichia coli, the transcription of the malT gene is activated by the complex formed between cAMP and its receptor protein, CRP. Kinetics of formation of polyribonucleotide products from the corresponding promoter were studied in vitro by two sets of techniques, abortive initiation assays and run-off experiments. The first type of assay indicated that open complexes were formed at malT with an equivalent efficiency, and at comparable rates, whether CRP-cAMP was present or not. Secondary effects due to the activating complex were observed (increased stability of the open complex, elimination of a weaker binding site for the enzyme, improved Michaelis constants of RNA polymerase for the substrates of the assay, UTP in particular). But, primarily, CRP-cAMP did not exert a significant role in the rate of formation of the initiation complex. In contrast, run-off assays showed that the yield of the full-length transcripts was markedly enhanced by prior incubation of the DNA fragment with CRP-cAMP. Both in the presence and in the absence of activator, the rate-limiting step for this process was markedly slower than the formation of the initial open complex. Short oligonucleotides (n less than 9), probably arising from a recycling process, were found when the initiation complex was formed in the absence of CRP-cAMP. They were abolished by prior incubation with the activator. Unexpectedly, CRP-cAMP appears to favour the escape of RNA polymerase from the initiation complex at this promoter.

Base Sequence↗

PubMed1993

Novel RNA polymerization reaction catalyzed by a group I ribozyme.

We have converted a bacterial tRNA precursor containing a 205 nt self-splicing group I intron into a RNA enzyme that catalyzes polymerization of an external RNA substrate. The reaction involves transesterification steps analogous to both the forward and reverse exon ligation steps of group I splicing; as such it depends entirely on 3' splice site reactions. The RNA substrate is a 20 nt analogue of the ligated exons (E1.E2), whose 3' end resembles the 3' terminus of the intron RNA enzyme (IVS). The splice junction of the substrate is attacked by the 3' end of the intron, then the molecule displaces the original 3' terminal guanosine so that the new 3' terminus is brought into the active site and used as the attacking nucleophile in the next reaction. Polymerization occurs via a series of covalent enzyme-linked intermediates of the structure IVS.(E2)n, where n = 1 to > or = 18. The 5' exon accumulates during the course of the reaction and can attack the covalent intermediates to produce elongation products of structure E1.(E2)n, regenerating the intron RNA enzyme in unchanged form. In this manner, the enzyme converts 20 nt oligoribonucleotides into polyribonucleotides up to at least 180 nt by 10 nt increments. These results have significant implications for the evolution of RNA-based self-replicating systems.

Adenosine Triphosphate↗

PubMed1976

Effects of RNase and RNA on in vitro aster assembly.

RNase alters the in vitro assembly of spindle asters in homogenates of meiotically dividing surf clam (Spisula solidissima) oocytes. Some effects of RNase, such as reduced astral fiber length, appear nonenzymatic and probably result from RNase binding to tubulin. However, RNase-induced changes in the microtubule organizing center are also observed. Since other polycations can mimic RNase effects, the existence of an RNA component of the spindle organizing center remains uncertain. Effects of RNase and other polycations on astral fiber length can be prevented and reversed by the RNase inhibitor, polyguanylic acid. Polyguanylic acid can also augment astral fiber length in the absence of added RNase or other polycations. Augmentation by polyguanylic acid is favored by high ionic strength, and can be duplicated by polyuridylic acid and, with less efficiency, by polyadenylic acid. Polycytidylic acid and unfractionated yeast RNA, however, are unable to augment aster assembly. Polyguanylic acid can also augment the length of astral fibers on complete spindles isolated under polymerizing conditions. These results demonstrate that specific polyribonucleotides can alter spindle assembly in vitro. The presence of an inhibitor of microtubule assembly in Spisula oocytes, which can be inactivated by specific RNAs, is suggested.

Animals↗

PubMed1986

Correlations between prostate chromatin structure and transcriptional activity and acceptor site distribution.

Androgen-receptor complexes are intimately involved in the maintenance of rat ventral prostate chromatin in a transcriptionally active structure. The presence or absence of androgens influenced the quantity of transcriptionally active chromatin and the distribution of acceptor sites for androgen-receptor complexes as probed by endonucleolytic cleavage. After castration, changes in the sedimentation rates of nucleosome oligomers were consistent with the absence of androgen-receptor complexes and elongating polyribonucleotide chains. These changes were accompanied by decreases in the ability of chromatin released under conditions of minimal nuclease digestion to bind androgen-receptor complexes and to support incorporation of RNA precursors responsive to androgenic stimulation. Saturation analyses of chromatin and nuclear fractions with partially purified androgen-receptor complexes revealed two affinity classes of acceptor sites. After castration, alterations in the intrachromatin distribution of acceptor sites were consistent with their redeployment into areas of decreased nuclease sensitivity, as previously shown for androgen-responsive genes.

Animals↗