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  • 1
    Electronic Resource
    Electronic Resource
    Deoxyribonucleic Acid Metabolism and Virus-Induced Enzyme Synthesis in a Thymine-Requiring Bacterium Infected by a Thymine-Requiring Bacteriophage* (1966)
    s.l. : American Chemical Society
    Biochemistry 5 (1966), S. 2092-2100 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00870a042
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  • 2
    Electronic Resource
    Electronic Resource
    Dihydrofolate reductases of Escherichia coli and bacteriophage T4. Spectrofluorometric study (1973)
    s.l. : American Chemical Society
    Biochemistry 12 (1973), S. 372-380 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00727a002
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  • 3
    Electronic Resource
    Electronic Resource
    DISCUSSION PAPER: BACTERIOPHAGE-INDUCED DIHYDROFOLATE REDUCTASE (1971)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 186 (1971), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1971.tb46960.x
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  • 4
    Electronic Resource
    Electronic Resource
    Protein–DNA interactions in the T4 dNTP synthetase complex dependent on gene 32 single-stranded DNA-binding protein (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 55 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Our laboratory has reported data suggesting a role for T4 phage gene 32 single-stranded DNA-binding protein in organizing a complex of deoxyribonucleotide-synthesizing enzymes at the replication fork. In this article we examined the effects of gene 32 ablation on the association of these enzymes with DNA–protein complexes. These experiments showed several deoxyribonucleotide-synthesizing enzymes to be present in DNA–protein complexes, with some of these associations being dependent on gene 32 protein. To further understand the role of gp32, we created amber mutations at codons 24 and 204 of gene 32, which encodes a 301-residue protein. We used the newly created mutants along with several experimental approaches – DNA-cellulose chromatography, immunoprecipitation, optical biosensor analysis and glutathione-S-transferase pulldowns – to identify relevant protein–protein and protein–DNA interactions. These experiments identified several proteins whose interactions with DNA depend on the presence of intact gp32, notably thymidylate synthase, dihydrofolate (DHF) reductase, ribonucleotide reductase (RNR) and Escherichia coli nucleoside diphosphate (NDP) kinase, and they also demonstrated direct associations between gp32 and RNR and NDP kinase, but not dCMP hydroxymethylase, deoxyribonucleoside monophosphate kinase, or DHF reductase. Taken together, the results support the hypothesis that the gene 32 protein helps to recruit enzymes of deoxyribonucleoside triphosphates synthesis to DNA replication sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04486.x
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  • 5
    Electronic Resource
    Electronic Resource
    Analysis of mutagenesis induced by a thermolabile T4 phage deoxycytidylate hydroxymethylase suggests localized deoxyribonucleotide pool imbalance (1991)
    Springer
    Molecular genetics and genomics 226 (1991), S. 257-264 
    Details
    ISSN: 1617-4623
    Keywords: Mutagenesis ; Replication fidelity ; Deoxyribonucleotide pools ; dCMP hydroxymethylase ; T4 bacteriophage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary To understand the molecular basis of mutation stimulated by deoxyribonucleotide pool imbalance, we studied a temperature-sensitive T4 phage gene 42 mutant (LB3), which specifies a thermolabile deoxycytidylate hydroxymethylase. Analysis of rII mutations, revertible to wild type along either GC-to-AT or AT-to-GC transition pathways, showed 8- to 80-fold stimulation of GC-to-AT mutations at a semi-permissive temperature (34° C). One such marker, rII SN103, which showed the highest stimulation at 34° C, was sequenced after amplification of the template by polymerase chain reaction. The mutant site in rII SN103 was identified at nucleotide position 265 from the rII B translational start as an AT-to-GC transition, which changes TCA to CCA. Sequence analysis of revertants and pseudorevertants generated at 34° C showed that both cytosines within this triplet can undergo change to either thymine or adenine, consistent with the hypothesis that hydroxymethyldeoxycytidine triphosphate pools are depleted at replication sites. However, dNTP pool measurements in extracts of 34° C cultures showed no significant deviations from values obtained at 30° C, suggesting that pool imbalances occur only locally, close to replication forks. Our studies support the hypothesis that the imitator phenotype displayed by ts LB3 at semi-permissive temperature is a consequence of perturbation of the flow of nucleotide precursors into the DNA replication machinery. A putative localized depletion of hm-dCTP presumably enlarges effective dTTP/hm-dCTP and dATP/hm-dCTP pool ratios, resulting in the observed C-to-T transition and C-to-A transversion mutations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00273611
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  • 6
    Electronic Resource
    Electronic Resource
    Ribonucleotide reductase: A determinant of 5-bromodeoxyuridine mutagenesis in phage T4 (1989)
    Springer
    Molecular genetics and genomics 217 (1989), S. 13-19 
    Details
    ISSN: 1617-4623
    Keywords: Ribonucleotide reductase ; 5-Bromodeoxyuridine ; Mutagenesis ; Deoxyribonucleotide pools ; Metabolic engineering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutagenesis by 5-bromodeoxyuridine (BrdUrd) can result from base-pairing errors either during replication of a BrdUrd-containing template or at the nucleotide incorporation step. Replication errors give rise predominantly to AT-to-GC transitions, while incorporation errors, in which 5-bromo-dUTP competes with dCTP at a template guanine site, should give rise to GC-to-AT transitions. The latter pathway should be sensitive to deoxyribonucleoside triphosphate (dNTP) pool fluctuations. Since dNTP pools are regulated through allosteric control of ribonucleotide reductase, the control of this enzyme should be a determinant of BrdUrd mutagenesis — if mutagenesis results largely from incorporation errors. Since T4 phage-encoded ribonucleotide reductase is insensitive to feedback inhibition, we established conditions under which phage DNA replication is dependent upon ribonucleotide reductase of the host, Escherichia coli. We examined BrdUrd mutagenesis of rII mutants known to revert to wild type either by AT-to-GC or GC-to-AT transition pathways. While both reversion pathways were stimulated under all conditions analyzed, the AT-to-GC pathway was stimulated more when the E. coli reductase was functioning, while the GC-to-AT pathway was more specifically enhanced when the T4 reductase was active. These results confirm that ribonucleotide reductase is a determinant of BrdUrd mutagenesis, but our observations, plus experiments showing that BrdUrd has relatively small effects upon dNTP pool sizes, indicate that the relationship between deoxyribonucleotide metabolism and BrdUrd mutagenesis is more complex than anticipated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330936
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  • 7
    Electronic Resource
    Electronic Resource
    Metabolic Functions of Microbial Nucleoside Diphosphate Kinases (2000)
    Springer
    Journal of bioenergetics and biomembranes 32 (2000), S. 259-267 
    Details
    ISSN: 1573-6881
    Keywords: NDP kinase ; adenylate kinase ; (dNTP:AMP) phosphotransferase ; CTP synthetase ; nucleotide pools ; mutator phenotype ; bacteriophage T4 ; dNTP synthetase complex ; anti-idiotypic antibody
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract This article summarizes research from our laboratory on two aspects of the biochemistry ofnucleoside diphosphate kinase from Escherichia coli—first, its interactions with several T4bacteriophage-coded enzymes, as part of a multienzyme complex for deoxyribonucleosidetriphosphate biosynthesis. We identify some of the specific interactions and discuss whetherthe complex is linked physically or functionally with the T4 DNA replicationmachinery, orreplisome. Second, we discuss phenotypes of an E. coli mutant strain carrying a targeteddeletion of ndk, the structural gene for nucleoside diphosphate kinase. How do bacteria lackingthis essential housekeeping enzyme synthesize nucleoside triphosphates? In view of the specificinteractions of nucleoside diphosphate kinase with T4 enzymes of DNA metabolism, howdoes T4 multiply after infection of this host? Finally, the ndk disruption strain has highlybiased nucleoside triphosphate pools, including elevations of the CTP and dCTP pools of7- and 23-fold, respectively. Accompanied by these biased nucleotide pools is a strong mutatorphenotype. What is the biochemical basis for the pool abnormalities and what are the mutagenicmechanisms? We conclude with brief references to related work in other laboratories.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005537013120
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  • 8
    Electronic Resource
    Electronic Resource
    T4 Phage deoxyribonucleoside triphosphate synthetase: Purification of an enzyme complex and identification of gene products required for integrityFinancial support for the this work came from National Institutes of Health Research Grant No. AI-15145. (1988)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 1 (1988), S. 48-57 
    Details
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: We have isolated a highly enriched preparation of the multienzyme complex which synthesize Deocyribonuleoside triphosphates (dNTPs) from bacteriophage T4-infected bacteria. By a combination of SDS polyacrylamide gel electrophoresis and assays for specific enzyme activities, we have been able to identify in our final preparation ten different gene products which were previously identified as constituents of this complex, based upon studies with crude preparation. The complex dissociates at high concentrations of NaCl and MgCl2 but is stable under ionic conditions thought to exits in vivo. The purified complex catalyzes the efficient five-step conversion of dCTP to dTTP. Experiments with several T4 mutants have demonstrated that gene product encoded by cd, regA, nrdA, and nrdB are necessary to retain physical integrity of the complex throughout the preparative procedure, while gp44, gp55, and gppseT are not required. We conclude from this evidence that the T4 early gene products which function in dNTP biosynthesis are, in fact, physically linked as a multienzyme complex, and that regA contributes to the integrity of this complex. However, the dNTP-synthesizing complex as we isolate it contains no detectable DNA polymerase, nor have other known replication proteins been detected.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300010109
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  • 9
    Electronic Resource
    Electronic Resource
    DNA precursor asymmetries, replication fidelity, and variable genome evolution (1992)
    New York, NY : Wiley-Blackwell
    BioEssays 14 (1992), S. 295-301 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Balanced pools of deoxyribonucleoside triphosphates (dNTPs) are essential for DNA replication to occur with maximum fidelity. Conditions that create biased dNTP pools stimulate mutagenesis, as well as other phenomena, such as recombination or cell death. In this essay we consider the effective dNTP concentrations at replication sites under normal conditions, and we ask how maintenance of these levels contributes toward the natural fidelity of DNA replication. We focus upon two questions. (1) In prokaryotic systems, evidence suggests that replication is driven by small, localized, rapidly replenished dNTP pools that do not equilibrate with the bulk dNTP pools in the cell. Since these pools cannot be analyzed directly, what indirect approaches can illuminate the nature of these replication-active pools? (2) In eukaryotic cells, the normal dNTP pools are highly asymmetric, with dGTP being the least abundant nucleotide. Moreover, the composition of the dNTP pools changes as cells progress through the cell cycle. To what extent might these natural asymmetries contribute toward a recently described phenomenon, the differential rate of evolution of different genes in the same genome?
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950140502
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