Role of DNA Polymerase I and the
            <i>rec</i>
            System in Excision-Repair in
            <i>Escherichia coli</i>

Cooper, Priscilla K.; Hanawalt, Philip C.

doi:10.1073/pnas.69.5.1156

Cited by 146 publications

(42 citation statements)

References 25 publications

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“…Inability to join interruptions resulting from dimer excision have been recently demonstrated for a vecA mutant (Yonei & NOZU, 1972). Because of the apparent role of the recAf gene in repair replication (Cooper & Hanawalt, 1972) we suggest that the uvr502 and recA mutations affect the resynthesis step of excision repair, which precedes final joining of single strand interruptions.…”

Section: Discussionmentioning

confidence: 99%

Ultraviolet Sensitivity, Spontaneous Mutability and DNA Degradation in Escherichia coli Strains Carrying Mutations in uvr and rec Genes

Smirnov

Filkova

Skavronskaya

1973

Journal of General Microbiology

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Escherichia coli uvr502 bacteria have a higher spontaneous mutability and are 4.6 times more u.v.-sensitive than isogenic wild-type bacteria. Bacteria deficient in dimer excision (uvrA6) are 15 times more u.v.-sensitive than isogenic uwAf bacteria. Double mutant uvrA6uvr5oz bacteria are only 1.5 times more u.v.-sensitive than uvrA6 bacteria and double mutant uvr502recA56 bacteria were as u.v.-sensitive as recA56 bacteria, suggesting that there exists a uvrA+-and recA+-dependent repair pathway which is blocked by the u v r~o z mutation. We suggest that the uvr5oa mutation affects primarily the excision repair pathway. Strict additivity of the uvr502 and recB21 mutations on U.V. sensitivity suggests that red+-mediated repair acts in part of repair pathway different from excision repair. U.v.-induced DNA degradation in the uvr502 bacteria is only slightly greater than that in uvr+ bacteria and the uvr502 mutation does not affect the 'reckless' character of u.v.-induced DNA breakdown in the recA56 bacteria. The uvr5oa-uvrA6 and uvr502recA56 or uvr5ozrecB21 double mutants have spontaneous mutation frequencies similar to that of the single uvr~oa strain.

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Section: Discussionmentioning

confidence: 99%

Ultraviolet Sensitivity, Spontaneous Mutability and DNA Degradation in Escherichia coli Strains Carrying Mutations in uvr and rec Genes

Smirnov

Filkova

Skavronskaya

1973

Journal of General Microbiology

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“…During DNA replication, Pol I joins the Okazaki fragments on the lagging strand of the replication fork (9,11). Pol I participates in excision repair by filling gaps resulting from the excision of damaged DNA bases (1,2). In addition, Pol I initiates the synthesis of certain plasmid DNAs in E. coli.…”

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confidence: 99%

DNA polymerase beta can substitute for DNA polymerase I in the initiation of plasmid DNA replication

1995

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We previously demonstrated that mammalian DNA polymerase ␤ can substitute for DNA polymerase I of Escherichia coli in DNA replication and in base excision repair. We have now obtained genetic evidence suggesting that DNA polymerase ␤ can substitute for E. coli DNA polymerase I in the initiation of replication of a plasmid containing a pMB1 origin of DNA replication. Specifically, we demonstrate that a plasmid with a pMB1 origin of replication can be maintained in an E. coli polA mutant in the presence of mammalian DNA polymerase ␤. Our results suggest that mammalian DNA polymerase ␤ can substitute for E. coli DNA polymerase I by initiating DNA replication of this plasmid from the 3 OH terminus of the RNA-DNA hybrid at the origin of replication.DNA polymerase I (Pol I) of Escherichia coli, encoded by the polA gene, functions in both DNA replication and DNA repair (3,8). During DNA replication, Pol I joins the Okazaki fragments on the lagging strand of the replication fork (9, 11). Pol I participates in excision repair by filling gaps resulting from the excision of damaged DNA bases (1, 2). In addition, Pol I initiates the synthesis of certain plasmid DNAs in E. coli. Enterobacterial plasmids containing a ColE1 or pMB1 origin of DNA replication are not maintained in several E. coli polA mutants, including the polA12 mutant (4, 7). Studies of plasmid DNA synthesis with purified proteins have demonstrated that the initiation of DNA replication at the ColE1 origin requires Pol I as well as RNA polymerase and RNase H (5). RNA polymerase transcribes RNA molecules, beginning approximately 555 bp upstream of the origin of DNA replication (6). The resulting RNA strand of the DNA-RNA hybrid is cleaved by RNase H, leaving a 3Ј OH terminus that serves as a primer for the initiation of DNA replication (10). Pol I initiates DNA synthesis from these primers, and it is replaced with the Pol III holoenzyme at a primosome assembly site approximately 400 nucleotides downstream from the origin (12, 16).We have previously shown that mammalian Pol ␤ is able to substitute for Pol I in DNA replication and in base excision repair (13,14). Pol ␤ increases the rate of joining of Okazaki fragments in a polA12(Ts) mutant at the nonpermissive temperature, suggesting that the Pol ␤ enzyme is able to fill gaps between the Okazaki fragments on the lagging strand (13). Expression of Pol ␤ in a polA12(Ts) mutant of E. coli confers methylmethane sulfonate resistance to this otherwise methylmethane sulfonate-sensitive strain, suggesting that Pol ␤ is able to fill gaps formed by the excision of alkylated bases (14). Therefore, we wished to determine whether Pol ␤ could also substitute for Pol I in the initiation of DNA replication of a plasmid containing a pMB1 origin of replication.The p␤ plasmid is maintained in a polA12 mutant. We initially observed that a plasmid that contains a pMB1 origin of replication, pMS119HE, was not maintained in a recA718 polA12(Ts) strain unless the strain was grown in medium containing ampicillin. However, the same pla...

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“…Similarly, the ATP-dependent deoxyribonuclease of M. smegmatis is similar to ATP-dependent deoxyribonucleases in E. coli and DlTplococcus pneumoniae (Winder & Lavin, 1971) and, hence, is likely to be involved in recombination repair (Rupp, Wilde, Reno & Howard-Flanders, I 971) and perhaps also excision repair (Cooper & Hanawalt, 1972). Hence, a reasonable hypothesis is that iron limitation and hydroxyurea treatment leads to the formation of abnormal DNA in M .…”

Section: Discussionmentioning

confidence: 99%

Effects of Hydroxyurea, Nalidixic Acid and Zinc Limitation on DNA Polymerase and ATP-dependent Deoxyribonuclease Activities of Mycobacterium smegmatis

Winder

Barber

1973

Journal of General Microbiology

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S U M M A R YTreatment of growing Mycobacterium smegmatis with hydroxyurea decreased the DNA/protein ratio and markedly increased the specific activities of DNA polymerase and ATP-dependent deoxyribonuclease. These changes were similar to those produced by iron limitation of growth. Treating M . srnegmatis with nalidixic acid also decreased the DNA/protein ratio but had no effect on the activity of either enzyme. Growth of M . srnegmatis under conditions of zinc limitation did not diminish the specific activity of DNA polymerase thus not favouring a role for zinc in the action of this enzyme. The activity of the ATP-dependent deoxyribonuclease was, however, slightly increased. In previous reports the specific activity of DNA polymerase in this organism has been seriously underestimated due to interfering deoxyribonuclease and nucleoside triphosphatase. This was corrected by sufficient dilution of the extract. Revised specific activities of DNA polymerase in carbon-limited, nitrogen-limited and iron-limited cultures are, respectively, 10, 14, I I and 64 units/mg protein.

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Role of DNA Polymerase I and the rec System in Excision-Repair in Escherichia coli

Cited by 146 publications

References 25 publications

Ultraviolet Sensitivity, Spontaneous Mutability and DNA Degradation in Escherichia coli Strains Carrying Mutations in uvr and rec Genes

Ultraviolet Sensitivity, Spontaneous Mutability and DNA Degradation in Escherichia coli Strains Carrying Mutations in uvr and rec Genes

DNA polymerase beta can substitute for DNA polymerase I in the initiation of plasmid DNA replication

Effects of Hydroxyurea, Nalidixic Acid and Zinc Limitation on DNA Polymerase and ATP-dependent Deoxyribonuclease Activities of Mycobacterium smegmatis

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