A nucleobase lesion remodels the interaction of its normal neighbor in a DNA glycosylase complex
Open accessAbstract
How DNA glycosylases search through millions of base pairs and discriminate between rare sites of damage and otherwise undamaged bases is poorly understood. Even less understood are the details of the structural states arising from DNA glycosylases interacting with undamaged DNA. Recognizing the mutagenic lesion 7,8-dihydro-8-oxoguanine (8-oxoguanine, oxoG) represents an especially formidable challenge, because this oxidized nucleobase differs by only two atoms from its normal counterpart, guanine (G), and buried in the structure of naked B-form DNA, oxoG and G are practically indistinguishable from each other. We have used disulfide cross-linking technology to capture a human oxoG repair protein, 8-oxoguanine DNA glycosylase I (hOGG1) sampling an undamaged G:C base pair located adjacent to an oxoG:C base pair in DNA. The x-ray structure of the trapped complex reveals that the presence of the 8-oxoG drastically changes the local conformation of the extruded G. The extruded but intrahelical state of the G in this structure offers a view of an early intermediate in the base-extrusion pathway.
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Structures of DNA in complex with OGG1 exist in a catalytically active form for 8oxoG that is adjacent to guanine only in the 5'-position in -AGGT- sequences.
“In fact, the structures of DNA in complex with N-glycosylase/DNA lyase (OGG1), which is a base-excision repair enzyme for 8oxoG, exist in a catalytically active form for 8oxoG that is adjacent to guanine only in the 5’-position in -AGGT- sequences (S12 Fig) [40,48–51].”
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REPAIR AND EFFECTS OF THE 8-OXOG LESION IN DNA
Covino, J. (2007) · The Mathematics Enthusiast
- Authors
- Banerjee, A., & Verdine, G. L.
- Affiliations
- Harvard University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2006-10-10
- Volume
- 103
- Issue
- 41
- Pages
- 15020-15025
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1622772
- OpenAlex
- W2069230847
- Cited by
- 48
- References
- 31
- Citations by year
- 2024: 1 · 2023: 1 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 3 · 2015: 1 · 2013: 1 · 2012: 8
- FWCI
- 1.77
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- Funders
- National Cancer Institute (R01CA100742)
- National Institute of General Medical Sciences (R01GM044853, GM 044853)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- 8-oxoguanine, OGG1, DNA glycosylase, GC base pairs, disulfide cross-linking, DNA repair, DNA conformation
- MeSH terms
- Binding Sites, DNA Damage, Guanine, Humans, Models, Chemical, Models, Molecular, Protein Conformation, Crystallography, X-Ray, DNA Glycosylases
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