Separation-of-function mutants unravel the dual-reaction mode of human 8-oxoguanine DNA glycosylase

Dalhus, Bjørn; Forsbring, Monika; Helle, Ina Høydal; Vik, Erik Sebastian; Forstrøm, Rune Johansen; Backe, Paul Hoff; Alseth, Ingrun; Bjørås, Magnar

doi:10.1016/j.str.2010.09.023

Cited by 89DNA Repair MechanismsDNA and Nucleic Acid ChemistryMetal-Catalyzed Oxygenation Mechanisms

Separation-of-function mutants unravel the dual-reaction mode of human 8-oxoguanine DNA glycosylase

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Dalhus, Bjørn, Forsbring, Monika, Helle, Ina Høydal, Vik, Erik Sebastian, Forstrøm, Rune Johansen, Backe, Paul Hoff, Alseth, Ingrun, Bjørås, Magnar·2011·Structure

DOI 10.1016/j.str.2010.09.023

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Abstract

7,8-Dihydro-8-oxoguanine (8oxoG) is a major mutagenic base lesion formed when reactive oxygen species react with guanine in DNA. The human 8oxoG DNA glycosylase (hOgg1) recognizes and initiates repair of 8oxoG. hOgg1 is acknowledged as a bifunctional DNA glycosylase catalyzing removal of the damaged base followed by cleavage of the backbone of the intermediate abasic DNA (AP lyase/β-elimination). When acting on 8oxoG-containing DNA, these two steps in the hOgg1 catalysis are considered coupled, with Lys249 implicated as a key residue. However, several lines of evidence point to a concurrent and independent monofunctional hydrolysis of the N-glycosylic bond being the in vivo relevant reaction mode of hOgg1. Here, we present biochemical and structural evidence for the monofunctional mode of hOgg1 by design of separation-of-function mutants. Asp268 is identified as the catalytic residue, while Lys249 appears critical for the specific recognition and final alignment of 8oxoG during the hydrolysis reaction.

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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].”
From Assessment of mutation probabilities of KRAS G12 missense mutants and their long-timescale dynamics by atomistic molecular simulations and Markov state modeling (2018) · cites this paper as [51]

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Authors: Dalhus, B., Forsbring, M., Helle, I. H., Vik, E. S., Forstrøm, R. J., Backe, P. H., Alseth, I., & Bjørås, M.
Affiliations: Oslo University Hospital (NO)
Corresponding author: Dalhus, Bjørn
ORCID: Dalhus, Bjørn
Forstrøm, Rune Johansen
Backe, Paul Hoff
Alseth, Ingrun
Bjørås, Magnar
Venue: Structure
Publisher: Elsevier BV
Published: 2011-01
Volume: 19
Issue: 1
Pages: 117-127
ISSN: 0969-2126 (ISSN-L)
DOI: 10.1016/j.str.2010.09.023
OpenAlex: W2082917187
Cited by: 89
References: 66
Citations by year: 2026: 3 · 2025: 5 · 2024: 6 · 2023: 7 · 2022: 8 · 2021: 3 · 2020: 9 · 2019: 7 · 2018: 7 · 2017: 9 · 2016: 3 · 2015: 3 · 2014: 3 · 2013: 4 · 2012: 10
FWCI: 2.46
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 928 d)
Locations: Structure (publishedVersion)
PubMed (publishedVersion)
Funders: Kreftforeningen
European Synchrotron Radiation Facility
Norges Forskningsråd
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 › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords: OGG1, 8-oxoguanine, base excision repair, separation-of-function mutants, abasic DNA, AP lyase activity, β-elimination, catalytic residues, DNA damage recognition, reactive oxygen species
MeSH terms: 8-Hydroxy-2'-Deoxyguanosine, Aspartic Acid, Binding Sites, Deoxyguanosine, Humans, Hydrolysis, Kinetics, Lyases, Polynucleotides, Protein Binding, Recombinant Fusion Proteins, Protein Structure, Tertiary, Crystallography, X-Ray, Catalytic Domain, DNA Glycosylases, DNA Cleavage

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Separation-of-function mutants unravel the dual-reaction mode of human 8-oxoguanine DNA glycosylase

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