Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.7.7 (DNA polymerase)
17,007 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Poly (2-methylthioinosinic acid) [poly(ms2I)] was found to markedly inhibit the RNA directed DNA polymerase (reverse transcriptase) activity of murine (Moloney, Rauscher) leukemia virus and murine (Moloney) sarcoma virus, while under the same conditions the unsubstituted parent compound poly(I) showed little, if any, inhibitory effect. Copolymers of inosinic acid (I) and 2-methylthioinosinic acid2(ms2I) showed an intermediary effect, depending on the I:ms2I ratio. Poly(ms2I) also inhibited the transformation of normal cells by murine (Moloney) sarcoma virus, as assessed by an infectious center assay.
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PMID:Inhibition of oncornavirus functions by poly (2-methylthioinosinic acid). 7 96

Chicken bone marrow cells transformed by reticuloendotheliosis virus (REV) produce in the cytoplasm a ribonucleoprotein (RNP) complex which has a sedimentation value of approximately 80 to 100S and a density of 1.23 g/cm3. This RNP complex is not derived from the mature virion. An endogenous RNA-directed DNA polymerase activity is associated with the RNP complex. The enzyme activity was completely neutralized by anti-REV DNA polymerase antibody but not by anti-avian myeloblastosis virus DNA polymerase antibody. The DNA product from the endogenous RNA-directed DNA polymerase reaction of the RNP complex hybridized to REV RNA but not to avian leukosis virus RNA. The RNA extracted from the RNP hybridized only to REV-specific complementary DNA synthesized from an endogenous DNA polymerase reaction of purified REV. The size of the RNA in the RNP is 30 to 35S, which represents the subunit size of the genomic RNA. No 60S mature genomic RNA was found within the RNP complex. The significance of finding the endogenous DNA polymerase activity in the viral RNP in infected cells and the maturation process of 60S virion RNA of REV are discussed.
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PMID:Isolation and characterization of a virus-specific ribonucleoprotein complex from reticuloendotheliosis virus-transformed chicken bone marrow cells. 8 19

We have adapted the chain-termination method for determining the nucleotide sequence of DNA of Sanger, Nicklen, and Coulson [(1977) Proc. Natl. Acad. Sci. USA 74, 5463--5467] for use with reverse transcriptase (RNA-directed DNA nucleotidyltransferase) on RNA templates. With this method and using a primer (the octanucleotide pdT7rC) directed at the 3'-terminal poly(A), we have determined a sequence of 166 residues in the genomic RNA of the picornavirus encephalomyocarditis virus.
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PMID:3'-terminal nucleotide sequence of encephalomyocarditis virus RNA determined by reverse transcriptase and chain-terminating inhibitors. 8 87

Adriamycin, daunomycin, acridylmethanesulfonanilide, and alkoxybenzophenanthridine alkaloids (coralyne acetosulfate, fagaronine chloride, and nitidine chloride) inhibit template-directed nucleic acid polymerizing enzyme activities like reverse transcriptase, DNA polymerase, and RNA polymerase. Enzyme reactions with poly(dA-dT), poly(rA)-oligo(dT) and poly(dA)-oligo(dT) are more strongly inhibited by the drugs than those with poly(dC)-poly(dG) and poly(rC)-oligo(dG). These results suggest that the antitumor drugs inhibit nucleic acid polymerases by a specific interaction with A:T base pairs of the templates.
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PMID:Base specificity in the inhibition of oncornavirus reverse transcriptase and cellular nucleic acid polymerases by antitumor drugs. 8 41

Phosphonoacetic acid has been shown to suppress replication of DNA tumor viruses by inhibiting the activity of virus-induced DNA polymerase and consequently viral DNA synthesis. We now have evidence to show that phosphonoacetic acid inhibits also the cellular DNA polymerases alpha, beta, and gamma of L1210 cells as well as reverse transcriptases of two type C viruses. Particularly, the DNA polymerase alpha is just as sensitive as the herpes virus induced DNA polymerase. The DNA polymerases beta and gamma required seven times more phosphonoacetic acid for a 50% inhibition of their activities. Phosphonoacetic acid inhibited the activities of the reverse transcriptase and terminal deoxyribonucleotidyltransferase only at higher concentrations. Kinetic analysis with the DNA polymerase alpha showed that the compound is a non-competitive inhibitor with respect to the substrates and uncompetitive inhibitor with the activated DNA template. Studies on time course of phosphonoacetic acid inhibition revealed that the compound is inhibitory even after the initiation of DNA synthesis. Phosphonoacetic acid also inhibited cell growth as well as the type C virus production; at concentrations above 50 microgram/ml, the inhibitory effect was more profound on the type C virus production than on cell growth.
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PMID:Inhibition of activities of DNA polymerase alpha, beta, gamma, and reverse transcriptase of L1210 cells by phosphonoacetic acid. 8 50

The IgG fraction of serum from a rabbit immunized with detergent-prepared human sperm nuclei inhibited the DNA polymerase activities in human sperm and seminal fluid as well as the partially purified reverse transcriptase of the baboon endogenous type-C retrovirus (BEV). The analogous enzymes from lysates of oncogenic type-C viruses was unaffected. IgG from the serum of individual partners from infertile marriages similarly inhibited both purified BEV reverse transcriptase and human sperm DNA polymerase, but not a DNA polymerase isolated from human prostatic fluid. The data suggest that BEV reverse transcriptase and the human sperm DNA polymerase are antigenically related. Furthermore, the sperm appears to be auto-antigenic and the antibodies thus formed may be capable of interfering with reproductive success.
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PMID:Inhibition of viral reverse transcriptase and human sperm DNA polymerase by anti-sperm antibodies. 8 98

The ability of reverse transcriptase to bind to [3H]tryptophanyl-tRNA and to function as DNA polymerase was compared for five temperature-sensitive mutants of avian sarcoma virus. Both activities of the reverse transcriptase were found to be heat labile in LA 335 and LA 336 as compared with the wild-type parents. For the other mutant viruses, LA 338, LA 343, and LA 672, grown at the permissive temperature, the reverse transcriptase was nearly as heat stable as for the wild-type parents in terms of tRNA binding and DNA polymerase. LA 338, LA 343, and LA 672 showed characteristic defects in their reverse transcriptase when propagated at the nonpermissive temperature; namely, tryptophanyl-tRNA binding and DNA polymerase activities were coordinately decreased in these virions. The reduced enzymatic activities were not entirely due to an inactive reverse transcriptase present in the virions, however, but rather lower amounts of enzyme protein incorporated into the virions contributed to the effect, according to assays of reverse transcriptase antigen by radioimmune competition.
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PMID:Binding of tryptophanyl-tRNA to the reverse transcriptase of replication-defective avian sarcoma viruses. 8 23

Sodium pyrophosphate inhibits synthesis of anticomplementary DNA during a reverse transcriptase (RNA-directed DNA nucleotidyltransferase, EC 2.7.7.7) catalyzed reaction. In the presence of pyrophosphate, the complementary DNA remains stably complexed to the RNA template. In the absence of pyrophosphate, the DNA. RNA hybrid template is degraded and anticomplementary DNA is synthesized. High concentrations of additives containing phosphodiester bonds appear to inhibit the ribonuclease H activity (hybrid nuclease, EC 3.1.4.34) of the reverse transcriptase, therby preventing formation of RNA primers necessary for the synthesis of anticomplementary DNA.
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PMID:Sodium pyrophosphate inhibition of RNA.DNA hybrid degradation by reverse transcriptase. 8 66

An RNA-direct DNA polymerase was purified from human melanoma tissue by successive column chromatography on DEAE-cellulose (DE-23 and DE-52) and phosphocellulose. The purified reverse transcriptase has a mol. wt. of 68,000, a pH optimum of 8.0, a Mn2+ optimum of 0.6 mM, and a KCl optimum of 60 mM. The purified enzyme transcribes (rA)n - (dT)12, (rC)n - (dG)18, (Ome-rC)n - (dG)18 and a 70s RNA from Rauscher leukemia virus (RLV), but failed to transcribe (dA)n - (dT)12. This enzyme has no terminal deoxynucleotidyl transferase activity. Serological studies have shown that the reverse transcriptase from human melanoma tissue is antigenically not related to DNA polymerases from Simian sarcoma virus (SiSV), Avian myeloblastosis virus (AMV), RLV, and human spleen of a patient with myelofibrosis. The purified enzyme showed a close antigenic resemblance to DNA polymerases from baboon endogenous virus (BEV) and rhabdomyosarcoma virus (RD-114), the endogenous virus of the cat.
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PMID:Biochemical and immunological characterization of a reverse transcriptase from human melanoma tissue. 8 88

Extracts from over 100 normal human placentas have been examined for RNA-directed DNA polymerase (DNA nucleotidyltransferase, EC 2.7.7.7) activity. More than 80% of these placentas contained this enzyme activity, which banded at a density of 1.15-1.17 g/ml in sucrose. After heat treatment, this enzyme activity was shifted in density to 1.22-1.24 g/ml. The enzymatic activity was greater with (rC)n.(dG)12-18 than with (dC)n.(dG)12-18 and was not stimulated by (dG)12-18 alone. The product of the endogenous reaction, which was sensitive to RNase, had the characteristics of a small DNA associated with a large RNA by hydrogen bonding. Electron microscopic inspection of the material with a density of 1.15-1.17 g/ml revealed numerous retrovirus-like particles with central electron-dense cores and double-membraned envelopes. The enzyme may be associated with the retrovirus-lik particles noted in the trophoblast layer of some human placentas.
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PMID:Normal human placentas contain RNA-directed DNA polymerase activity like that in viruses. 8 52


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