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)

The effect of different doses of N-methyl-N-nitrosourea (MNU) on a viability of bacterial cells with different defects in the systems of repair of UV-damages, and the MNU induction of single-strand DNA breaks (SS) were studied. The kinetics of both processes was investigated. There was a good correlation between the NMU sensitivity of bacterial cells and the number of SS in their DNAs. The most sensitive were the cells defective in DNA polymerase I. The optimal conditions for DNA repair in the strains under investigation were established. 90% of MNU-induced SS are repaired by DNA polymerase I and do not depend on protein synthesis. On the other hand, the exrA and recA dependent ways of SS repair depend on protein synthesis. The existence of an inducible recAexrA-dependent repair system of NMU-induced lesions in bacterial DNA is proposed.
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PMID:[Effect of B polA1- exrA- and recA-gene mutations on the reparation of single-strand DNA breaks induced by N-nitrosomethylurea]. 36 9

An RNA-directed DNA polymerase was purified from mouse spleen infected with leukaemia virus activated during N-methyl-N-nitroso urea- (MNU-) induced leukaemogenesis. The enzyme was isolated from the microsomal fraction and purified by successive chromatography of Sephadex G-200 and phosphocellulose. Estimation of molecular weight from the sedimentation rate of the purified enzyme in a sucrose gradient gave a value of 70,000. The enzyme had a pH optimum of 7.4, a KC1 optimum of 50 mmol/l, an Mn2+ optimum of 0.2 mmol/l, and a temperature optimum of 25 degrees C, when (rA)n . (dT) 10 was used as the template-primer. It preferred (rA)n . (dT)10 as the template-primer and transcribed (rC)n . (dG) 12 and (OMeC)n . (dG)12. A comparison of the properties of this DNA polymerase with the enzyme purified from murine type C retroviruses showed that the MNU-activated virus enzyme was both biochemically and biophysically indistinguishable from murine leukaemia virus DNA polymerases.
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PMID:Characterization of an RNA-directed DNA polymerase from mouse spleen infected with leukaemia virus activated during N-methyl-N-nitroso urea-induced leukaemogenesis. 617 78

Alkylatio of Escherichia coli DNA that have been made permeable to nucleotides by toluene treatment results in the expression of DNA polymerase I-directed repair synthesis. The system only permits measurement of DNA polymerase I-directed repair synthesis. The latter is not observed in mutant cells deficient in this polymerase. DNA ligation is intentionally prevented by the addition of the inhibitor, nicotinamide mononucleotide. MNU, ENU and MMS elicit DNA polymerase I-directed repair synthesis. MNU and MMS are especially potent in this regard, while EMS is a poor inducer of DNA polymerase I activity in permeabilized cells. The natural compound para-aminobenzoic acid itself (0,0002 mM - 20 mM) doesn't induce DNA polymerase I-directed repair synthesis. However, when PABA is used in complex with alkylating agents as the inducers, the repair synthesis increased 2,0, 1,2 and 2,8 times for MNU, ENU and EMS, respectively, as compared to that elicited by "pure" mutagens. The increasing of DNA repair synthesis in permeabilized bacteria in the experiments with PABA may serve as the foundation for its reparagenic activity. The latter was discovered previously by the authors in experiments on mutagenesis of bacterial cells.
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PMID:[Genetic activity of para-aminobenzoic acid. The intensification of DNA polymerase I-dependent repair induced by chemical mutagens in toluene-treated Escherichia coli cells]. 704 62

The DNA damage dependence of poly(ADP-ribose) polymerase-2 (PARP-2) activity is suggestive of its implication in genome surveillance and protection. Here we show that the PARP-2 gene, mainly expressed in actively dividing tissues follows, but to a smaller extent, that of PARP-1 during mouse development. We found that PARP-2 and PARP-1 homo- and heterodimerize; the interacting interfaces, sites of reciprocal modification, have been mapped. PARP-2 was also found to interact with three other proteins involved in the base excision repair pathway: x-ray cross complementing factor 1 (XRCC1), DNA polymerase beta, and DNA ligase III, already known as partners of PARP-1. XRCC1 negatively regulates PARP-2 activity, as it does for PARP-1, while being a polymer acceptor for both PARP-1 and PARP-2. To gain insight into the physiological role of PARP-2 in response to genotoxic stress, we developed by gene disruption mice deficient in PARP-2. Following treatment by the alkylating agent N-nitroso-N-methylurea (MNU), PARP-2-deficient cells displayed an important delay in DNA strand breaks resealing, similar to that observed in PARP-1 deficient cells, thus confirming that PARP-2 is also an active player in base excision repair despite its low capacity to synthesize ADP-ribose polymers.
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PMID:Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. 1194 90