The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Roles of E. coli DNA polymerases IV and V in lesion-targeted and untargeted SOS mutagenesis
Abstract
The expression of the Escherichia coli DNA polymerases pol V (UmuD'2C complex) and pol IV (DinB) increases in response to DNA damage. The induction of pol V is accompanied by a substantial increase in mutations targeted at DNA template lesions in a process called SOS-induced error-prone repair. Here we show that the common DNA template lesions, TT (6-4) photoproducts, TT cis-syn photodimers and abasic sites, are efficiently bypassed within 30 seconds by pol V in the presence of activated RecA protein (RecA*), single-stranded binding protein (SSB) and pol III's processivity beta,gamma-complex. There is no detectable bypass by either pol IV or pol III on this time scale. A mutagenic 'signature' for pol V is its incorporation of guanine opposite the 3'-thymine of a TT (6-4) photoproduct, in agreement with mutational spectra. In contrast, pol III and pol IV incorporate adenine almost exclusively. When copying undamaged DNA, pol V exhibits low fidelity with error rates of around 10(-3) to 10(-4), with pol IV being 5- to 10-fold more accurate. The effects of RecA protein on pol V, and beta,gamma-complex on pol IV, cause a 15,000- and 3,000-fold increase in DNA synthesis efficiency, respectively. However, both polymerases exhibit low processivity, adding 6 to 8 nucleotides before dissociating. Lesion bypass by pol V does not require beta,gamma-complex in the presence of non-hydrolysable ATPgammaS, indicating that an intact RecA filament may be required for translesion synthesis.
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“These multiplet mutations are likely the consequence of error-prone bypass polymerization during translesion synthesis and are consistent with the processivity of bypass polymerases persisting for several nucleotides after the bypass-requiring blocking lesion (39 -41).”
From Why Cockayne syndrome patients do not get cancer despite their DNA repair deficiency (2016) · cites this paper as [41]
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Cites
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UmuD′ 2 C is an error-prone DNA polymerase, Escherichia coli pol V
Tang, M., Shen, X., Frank, E. G., O’Donnell, M. E., Woodgate, R., & Goodman, M. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.8919 · Cited by 537
Self-citationThe dinB Gene Encodes a Novel E. coli DNA Polymerase, DNA Pol IV, Involved in Mutagenesis
Wagner, J. E., Grúz, P., Kim, S.-R., Yamada, M., Matsui, K., Fuchs, R. P., & Nohmi, T. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80376-7 · Cited by 474
Reuven, N. B., Arad, G., Maor-Shoshani, A., & Livneh, Z. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.31763 · Cited by 372
Kim, S.-R., Maenhaut-Michel, G., Yamada, M., Yamamoto, Y., Matsui, K., Sofuni, T., Nohmi, T., & Ohmori, H. (1997) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.94.25.13792 · Cited by 343
Knippers, R. (1970) · Nature · doi:10.1038/2281050a0 · Cited by 323
Interaction of recA protein with single-stranded DNA
Menetski, J. P., & Kowalczykowski, S. C. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90092-0 · Cited by 313
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- Creighton,S., Bloom,L. B. & Goodman, M. F. in Methods Enzymol. Vol. 262 (ed. Campbell, J. L.) 232–256 (Academic, San Diego, 1995).
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Error-Prone Repair DNA Polymerases in Prokaryotes and Eukaryotes
Goodman, M. F. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.083101.124707 · Cited by 727
Self-citationMutation as a Stress Response and the Regulation of Evolvability
Galhardo, R. S., Hastings, P. J., & Rosenberg, S. M. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701648502 · Cited by 643
The contribution of endogenous sources of DNA damage to the multiple mutations in cancer
Jackson, A. L., & Loeb, L. A. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00091-4 · Cited by 640
Crystal Structure of a Y-Family DNA Polymerase in Action
Ling, H., Boudsocq, F., Woodgate, R., & Yang, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00515-3 · Cited by 610
Self-citationInhibition of Mutation and Combating the Evolution of Antibiotic Resistance
Cirz, R. T., Chin, J. K., Andes, D. R., de Crécy‐Lagard, V., Craig, W. A., & Romesberg, F. E. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030176 · Cited by 583
Metadata
- Authors
- Tang, M., Pham, P., Shen, X., Taylor, J.-S., O'Donnell, M., Woodgate, R., & Goodman, M. F.
- Affiliations
- University of Southern California (US)
- Washington University in St. Louis (US)
- National Institutes of Health (US)
- Corresponding author
- Goodman, Myron F.
- Venue
- Nature
- Published
- 2000-04
- Volume
- 404
- Issue
- 6781
- Pages
- 1014-1018
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1510371408
- Cited by
- 443
- References
- 30
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 6 · 2023: 5 · 2022: 7 · 2021: 5 · 2020: 9 · 2019: 6 · 2018: 12 · 2017: 14 · 2016: 10 · 2015: 10 · 2014: 19 · 2013: 13 · 2012: 21
- FWCI
- 16.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Carcinogens and Genotoxicity Assessment
- Keywords
- DNA polymerase IV, DNA polymerase V, DinB, SOS response, error-prone DNA repair, translesion synthesis, 6-4 photoproducts, abasic sites, RecA filament, polymerase fidelity, mutational signatures, DNA damage response
- MeSH terms
- DNA Damage, DNA-Directed DNA Polymerase, DNA, Bacterial, Escherichia coli, Rec A Recombinases, SOS Response, Genetics, Templates, Genetic, Mutagenesis, DNA Polymerase beta, Escherichia coli Proteins
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