characterization of the escherichia coli uracil-dna glycosylase.inhibitor protein complex.the bacillus subtilis bacteriophage pbs2 uracil-dna glycosylase inhibitor (ugi) protein was characterized and shown to form a stable complex with escherichia coli uracil-dna glycosylase (ung). as determined by mass spectrometry, the ugi protein had a molecular weight of 9,474. we confirmed this value by sedimentation equilibrium centrifugation and determined that ugi exists as a monomeric protein in solution. amino acid analysis performed on both ugi and ung proteins was in excellent agreement w ...19921429601
enzymatic degradation of uracil-containing dna. ii. evidence for n-glycosidase and nuclease activities in unfractionated extracts of bacillus subtilis.further studies have confirmed our earlier observations that in the presence of edta, degradation of phage pbs2 [3h]uracil-labeled dna is effected by an n-glycosidase activity in extracts of bacillus subtilis that removes free uracil from dna. in addition, such extracts contain a nuclease activity that attacks pbs2 dna in the presence of cacl2. the nuclease activity is not observed under conditions that inactivate n-glycosidase activity but does attack dna that has been preincubated to remove ur ...1976822172
relationship of bacillus subtilis dna polymerase iii to bacteriophage pbs2-induced dna polymerase and to the replication of uracil-containing vivo studies of pbs2 phage replication in a temperature-sensitive bacillus subtilis dna polymerase iii (pol iii) mutant and a temperature-resistant revertant of this mutant have suggested the possible involvement of pol iii in pbs2 dna synthesis. previous results with 6-(p-hydroxyphenylazo)-uracil (hpura), a specific inhibitor of pol iii and dna replication in uninfected cells, suggest that pol iii is not involved in phage dna replication, due to its resistance to this drug. experiments were ...1978104052
metabolism of uracil-containing dna: degradation of bacteriophage pbs2 dna in bacillus subtilis.when bacillus subtilis is infected by the uracil-containing dna phage pbs2, the parental dna labeled with radioactive uracil and cytosine remains acid insoluble. if the synthesis of the phage-induced uracil-dna n-glycosidase inhibitor is prevented, the parental dna is completely degraded to acid-soluble products beginning at about 6 min after infection. the host n-glycosidase probably initiates the degradation pathway, with nucleases being responsible for the remaining degradation of the dna.1977406424
transcriptional specificity of a multisubunit rna polymerase induced by bacillus subtilis bacteriophage pbs2.bacillus subtilis phage pbs2 induced the synthesis of two temporally defined categories of phage-specified transcripts. the transcription of phage "early" genes was induced almost immediately after infection; this rna synthesis did not require phage protein synthesis. phage "late" gene transcription, on the other hand, was induced at an intermediate time in the lytic cycle; this rna synthesis required the production of phage proteins. both classes of transcription were resistant to the drug rifa ...1978413936
bacillus subtilis deoxyuridinetriphosphatase and its bacteriophage pbs2-induced inhibitor.extracts of bacillus subtilis contain a deoxyuridinetriphosphatase (dutpase) activity with a molecular weight of approximately 48,000. the enzyme is maximally active at ph 8.5, being stimulated by mg2+ and inhibited by edta. the enzyme is specific for dutp among all the natural nucleotides tested, with an apparent km for dutp of 2 mum. bacteriophage pbs2, whose dna contains uracil instead of thymine, induces upon infection of b. subtilis a new 83,000-dalton protein which inhibits the host's dutp ...1975810487
bacteriophage pbs2-induced inhibition of uracil-containing dna degradation.degradation of uracil-containing dna by bacillus subtilis extracts and its inhibition after infection by the uracil-containing dna phage pbs2 have been investigated to resolve differences between the published reports of tomita and takahashi (1975) and friedberg et al. (1975, 1976). the product of hydrolysis of pbs2 dna, tritium labeled in its uracil and cytosine residues, is solely uracil and not deoxyuridine. the degrading activity is completely inhibited within 7 min after pbs2 infection, bef ...1976824463
bacteriophage transformation of pbs2 in bacillus subtilis.transformation of temperature-sensitive mutants of bacteriophage pbs2 for bacillus subtilis was demonstrated. the number of transformants was linearly related to the concentration of dna within a range of 0.01 to 1 mug/ml. no transformants were obtained when the dna was pretreated with dnase. pbs2 dna sheared to approximately 1% of the total chromosome length was centrifuged in cs2so4-hg gradients to fractionate the dna according to the base composition. transformation experiments carried out wi ...1975803565
resistance of bacteriophage pbs2 infection to rifampicin, an inhibitor of bacillus subtilis rna synthesis. 19724404678
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