The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Exonuclease III and endonuclease IV remove 3' blocks from DNA synthesis primers in H2O2-damaged Escherichia coli.
Open accessAbstract
Escherichia coli deficient in exonuclease III (xth gene mutants) are known to be hypersensitive to hydrogen peroxide. We now show that such mutants accumulate many more DNA single-strand breaks than do wild-type bacteria upon exposure to H2O2. DNA isolated from H2O2-treated xth- cells contains strand breaks that do not efficiently support synthesis by E. coli DNA polymerase I, indicating the presence of blocking groups at the DNA 3' termini. Purified E. coli exonuclease III activates this blocked DNA to allow substantial synthesis by polymerase I in vitro. Another E. coli enzyme, endonuclease IV, also activates primers for DNA polymerase. Exonuclease III accounts for greater than 95% of the total activity in E. coli crude extracts for removal of 3'-terminal phosphoglycolaldehyde esters from model DNA substrates. Purified exonuclease III and endonuclease IV can each efficiently remove 3'-terminal phosphoglycolaldehyde in vitro. An important physiological function for exonuclease III is thus the activation of blocked 3' ends for DNA repair synthesis. Endonuclease IV can also initiate the repair of ruptured 3'-deoxyribose in DNA.
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Cites
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DNA damage and oxygen radical toxicity
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Self-citationClustered DNA damages induced in isolated DNA and in human cells by low doses of ionizing radiation
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Metadata
- Authors
- Demple, B., Johnson, A., & Fung, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1986-10
- Volume
- 83
- Issue
- 20
- Pages
- 7731-7735
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1983700730
- Cited by
- 275
- References
- 26
- FWCI
- 4.97
- Type
- journal article
- Language
- en
- Open access
- green
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- Demple, B., Johnson, A., & Fung, D. (1986). Exonuclease III and endonuclease IV remove 3' blocks from DNA synthesis primers in H2O2-damaged Escherichia coli. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.83.20.7731
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