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NH2-terminal Proline Acts as a Nucleophile in the Glycosylase/AP-Lyase Reaction Catalyzed by Escherichia coli Formamidopyrimidine-DNA Glycosylase (Fpg) Protein
Open accessAbstract
Formamidopyrimidine-DNA glycosylase (Fpg) protein plays a prominent role in the repair of oxidatively damaged DNA in Escherichia coli. The protein possesses three enzymatic activities, hydrolysis of the N-glycosidic bond (DNA glycosylase), beta-elimination (AP lyase), and delta-elimination; these functions act in a concerted manner to excise oxidized deoxynucleosides from duplex DNA. Schiff base formation between the enzyme and substrate has been demonstrated (Tchou, J., and Grollman, A. P. (1995) J. Biol. Chem. 270, 11671-11677); this protein-DNA complex can be trapped by reduction with sodium borohydride. By digesting the stable, covalently linked intermediate with proteases and determining the accurate mass of the products by negative electrospray ionization-mass spectrometry, we show that the N-terminal proline of Fpg protein is linked to DNA and, therefore, is identified as the nucleophile that initiates the catalytic excision of oxidized bases from DNA. This experimental approach may be applicable to the analysis of other protein-DNA complexes.
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Citations
Cited by
Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase
Rosenquist, T. A., Zharkov, D. O., & Grollman, A. P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7429 · Cited by 485
Self-citationA Mechanistic Perspective on the Chemistry of DNA Repair Glycosylases
Stivers, J. T., & Jiang, Y. L. (2003) · Chemical Reviews · doi:10.1021/cr010219b · Cited by 447
Enzymatic Processing of Radiation-Induced Free Radical Damage in DNA
Wallace, S. S. (1998) · Radiation Research · doi:10.2307/3579809 · Cited by 334
Lu, R., Nash, H. M., & Verdine, G. L. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00187-4 · Cited by 323
Investigations of pyrimidine dimer glycosylases—A paradigm for DNA base excision repair enzymology
Lloyd, R. S. (2005) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2005.04.003 · Cited by 37
Metadata
- Authors
- Zharkov, D. O., Rieger, R. A., Iden, C. R., & Grollman, A. P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-02
- Volume
- 272
- Issue
- 8
- Pages
- 5335-5341
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2113104146
- Cited by
- 180
- References
- 0
- FWCI
- 5.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: NH2-terminal Proline Acts as a Nucleophile in the Glycosylase/AP-Lyase Reaction Catalyzed by Escherichia coli Formamidopyrimidine-DNA Glycosylase (Fpg) Protein. https://app.cochat.ai/papers/10.1074/jbc.272.8.5335
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- Zharkov, D. O., Rieger, R. A., Iden, C. R., & Grollman, A. P. (1997). NH2-terminal Proline Acts as a Nucleophile in the Glycosylase/AP-Lyase Reaction Catalyzed by Escherichia coli Formamidopyrimidine-DNA Glycosylase (Fpg) Protein. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.8.5335
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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