The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation.
Open accessAbstract
The products of the SOS-regulated umuDC operon are required for most UV and chemical mutagenesis in Escherichia coli. It has been shown that the UmuD protein shares homology with LexA, the repressor of the SOS genes. In this paper we describe a series of genetic experiments that indicate that the purpose of RecA-mediated cleavage of UmuD at its bond between Cys-24 and Gly-25 is to activate UmuD for its role in mutagenesis and that the COOH-terminal fragment of UmuD is necessary and sufficient for the role of UmuD in UV mutagenesis. Other genetic experiments are presented that (i) support the hypothesis that the primary role of Ser-60 in UmuD function is to act as a nucleophile in the RecA-mediated cleavage reaction and (ii) raise the possibility that RecA has a third role in UV mutagenesis besides mediating the cleavage of LexA and UmuD.
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Cites
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Ultraviolet mutagenesis and inducible DNA repair in Escherichia coli
Witkin, E. M. (1976) · Bacteriological Reviews · doi:10.1128/br.40.4.869-907.1976 · Cited by 1,862
Mutagenesis and inducible responses to deoxyribonucleic acid damage in Escherichia coli
Walker, G. C. (1984) · Microbiological Reviews · doi:10.1128/mmbr.48.1.60-93.1984 · Cited by 1,770
Self-citationThe SOS regulatory system of Escherichia coli
Little, J. W., & Mount, D. W. (1982) · Cell · doi:10.1016/0092-8674(82)90085-x · Cited by 1,489
Walker, G. C. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.002233 · Cited by 571
Self-citationKato, T., & Shinoura, Y. (1977) · Molecular and General Genetics MGG · doi:10.1007/bf00283484 · Cited by 568
Cleavage of the Escherichia coli lexA protein by the recA protease.
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Autodigestion of lexA and phage lambda repressors.
Little, J. W. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.5.1375 · Cited by 508
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Homology among DNA-binding proteins suggests use of a conserved super-secondary structure
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Cited by
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
PROTEASES AND THEIR TARGETS IN ESCHERICHIA COLI
Gottesman, S. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.465 · Cited by 717
Y-family DNA polymerases and their role in tolerance of cellular DNA damage
Sale, J. E., Lehmann, A. R., & Woodgate, R. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3289 · Cited by 665
SSB as an Organizer/Mobilizer of Genome Maintenance Complexes
Shereda, R. D., Kozlov, A. G., Lohman, T. M., Cox, M. M., & Keck, J. L. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230802341296 · Cited by 553
Kogoma, T. (1997) · Microbiology and molecular biology reviews : MMBR · doi:10.1128/.61.2.212-238.1997 · Cited by 532
Metadata
- Authors
- Nohmi, T., Battista, J. R., Dodson, L. A., & Walker, G. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1988-03
- Volume
- 85
- Issue
- 6
- Pages
- 1816-1820
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2001952964
- Cited by
- 408
- References
- 33
- FWCI
- 10.80
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation. https://app.cochat.ai/papers/10.1073/pnas.85.6.1816
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- Nohmi, T., Battista, J. R., Dodson, L. A., & Walker, G. C. (1988). RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.85.6.1816
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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