ArticleThe FEBS journal2017
An unconventional family 1 uracil DNA glycosylase in Nitratifractor salsuginis.
Article in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 7 citations in OpenAlex.
- Center Degenerated Walking-Primer PCR: A Novel and Universal Genome-Walking Method.Current issues in molecular biology · 2025Article
- Uracil walking primer PCR: An accurate and efficient genome-walking tool.Journal, genetic engineering & biotechnology · 2025Article
- Structural and functional coupling in cross-linking uracil-DNA glycosylase UDGX.Bioscience reports · 2024Article
- Role of endonuclease III enzymes in uracil repair.Mutation research · 2019Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The uracil DNA glycosylase superfamily consists of at least six families with a diverse specificity toward DNA base damage. Family 1 uracil N-glycosylase (UNG) exhibits exclusive specificity on uracil-containing DNA. Here, we report a family 1 UNG homolog from Nitratifractor salsuginis with distinct biochemical features that differentiate it from conventional family 1 UNGs. Globally, the crystal structure of N. salsuginisUNG shows a few additional secondary structural elements. Biochemical and enzyme kinetic analysis, coupled with structural determination, molecular modeling, and molecular dynamics simulations, shows that N. salsuginisUNG contains a salt bridge network that plays an important role in DNA backbone interactions. Disruption of the amino acid residues involved in the salt bridges greatly impedes the enzymatic activity. A tyrosine residue in motif 1 (GQDPY) is one of the distinct sequence features setting family 1 UNG apart from other families. The crystal structure of Y81G mutant indicates that several subtle changes may account for its inactivity. Unlike the conventional family 1 UNG enzymes, N. salsuginisUNG is not inhibited by Ugi, a potent inhibitor specific for family 1 UNG. This study underscores the diversity of paths that a uracil DNA glycosylase may take to acquire its unique structural and biochemical properties during evolution. DATABASE: Structure data are available in the PDB under accession numbers 5X3G and 5X3H.
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Registered trials
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