ArticleNature chemical biology2019
Suicide inactivation of the uracil DNA glycosylase UdgX by covalent complex formation.
Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Structural basis of DNA replication fidelity of the Mpox virus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular Biology Applications of Psychrophilic Enzymes: Adaptations, Advantages, Expression, and Prospective.Applied biochemistry and biotechnology · 2024Review
- Structural and functional coupling in cross-linking uracil-DNA glycosylase UDGX.Bioscience reports · 2024Article
- Mutational and structural analyses of UdgX: insights into the active site pocket architecture and its evolution.Nucleic acids research · 2023Article
- HMGN1 enhances CRISPR-directed dual-function A-to-G and C-to-G base editing.Nature communications · 2023Article
- DR0022 from Deinococcus radiodurans is an acid uracil-DNA glycosylase.The FEBS journal · 2022Article
- Bacterial DNA excision repair pathways.Nature reviews. Microbiology · 2022Review
- Efficient C•G-to-G•C base editors developed using CRISPRi screens, target-library analysis, and machine learning.Nature biotechnology · 2021Article
- Detection of Genomic Uracil Patterns.International journal of molecular sciences · 2021Review
- Visualization of uracils created by APOBEC3A using UdgX shows colocalization with RPA at stalled replication forks.Nucleic acids research · 2020Article
- Catalytic mechanism of the mismatch-specific DNA glycosylase methyl-CpG-binding domain 4.The Biochemical journal · 2020Article
- DNA-Protein Cross-Link Formation in Nucleosome Core Particles Treated with Methyl Methanesulfonate.Chemical research in toxicology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A uracil DNA glycosylase (UDG) from Mycobacterium smegmatis (MsmUdgX) shares sequence similarity with family 4 UDGs and forms exceedingly stable complexes with single-stranded uracil-containing DNAs (ssDNA-Us) that are resistant to denaturants. However, MsmUdgX has been reported to be inactive in excising uracil from ssDNA-Us and the underlying structural basis is unclear. Here, we report high-resolution crystal structures of MsmUdgX in the free, uracil- and DNA-bound forms, respectively. The structural information, supported by mutational and biochemical analyses, indicates that the conserved residue His109 located on a characteristic loop forms an irreversible covalent linkage with the deoxyribose at the apyrimidinic site of ssDNA-U, thus rendering the enzyme unable to regenerate. By proposing the catalytic pathway and molecular mechanism for MsmUdgX, our studies provide an insight into family 4 UDGs and UDGs in general.
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