ArticleJournal of the American Chemical Society2009
Efficient recognition of an unpaired lesion by a DNA repair glycosylase.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Human MutLα activates methylpurine DNA glycosylase to induce alkylation damage cytotoxicity.bioRxiv : the preprint server for biology · 2025Article
- Highly sensitive and high-throughput detection of human alkyladenine DNA glycosylase via hybridization chain reaction-assisted quantum dot fluorescent assay.Analytical and bioanalytical chemistry · 2025Article
- Multifaceted nucleic acid probing with a rationally upgraded molecular rotor.Chemical science · 2024Article
- Gene editing with 'pencil' rather than 'scissors' in human pluripotent stem cells.Stem cell research & therapy · 2023Review
- Generation of 3'-OH terminal-triggered encoding of multicolor fluorescence for simultaneous detection of different DNA glycosylases.Analytical and bioanalytical chemistry · 2022Article
- Efficient DNA fluorescence labeling via base excision trapping.Nature communications · 2022Article
- Computational investigations on target-site searching and recognition mechanisms by thymine DNA glycosylase during DNA repair process.Acta biochimica et biophysica Sinica · 2022Review
- Rolling circle amplification-driven encoding of different fluorescent molecules for simultaneous detection of multiple DNA repair enzymes at the single-molecule level.Chemical science · 2020Article
- DNA aptamers against the DUX4 protein reveal novel therapeutic implications for FSHD.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Recognition of 1,The Journal of biological chemistry · 2020Article
- A single quantum dot-based nanosensor with multilayer of multiple acceptors for ultrasensitive detection of human alkyladenine DNA glycosylase.Chemical science · 2019Article
- Distinguishing Specific and Nonspecific Complexes of Alkyladenine DNA Glycosylase.Biochemistry · 2018Article
- Simultaneous sensitive detection of multiple DNA glycosylases from lung cancer cells at the single-molecule level.Chemical science · 2018Article
- Search for DNA damage by human alkyladenine DNA glycosylase involves early intercalation by an aromatic residue.The Journal of biological chemistry · 2017Article
- Mechanisms of glycosylase induced genomic instability.PloS one · 2017Article
- High-resolution Digital Mapping of N-Methylpurines in Human Cells Reveals Modulation of Their Induction and Repair by Nearest-neighbor Nucleotides.The Journal of biological chemistry · 2015Article
- Probing the DNA structural requirements for facilitated diffusion.Biochemistry · 2015Article
- Isolating contributions from intersegmental transfer to DNA searching by alkyladenine DNA glycosylase.The Journal of biological chemistry · 2013Article
- Recent advances in the structural mechanisms of DNA glycosylases.Biochimica et biophysica acta · 2013Review
- Surprising repair activities of nonpolar analogs of 8-oxoG expose features of recognition and catalysis by base excision repair glycosylases.Journal of the American Chemical Society · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The duplex structure of DNA, with its internal base pairing, protects the nucleobases from chemical damage, but it also poses a barrier to DNA-modifying enzymes, including the enzymes that recognize and repair DNA damage. It is known that unpaired (or bulged) nucleotides are significantly more accessible, but it is not known whether they might be recognized by nucleotide-flipping enzymes. We have investigated this question with human alkyladenine DNA glycosylase (AAG). AAG recognizes a wide variety of structurally disparate lesions, including deoxyinosine (I), which results from the spontaneous oxidative deamination of adenosine, and catalyzes the hydrolysis of the N-glycosidic bond to release the lesion base and initiate the base excision repair pathway. We used single-turnover kinetics to characterize the reactions of AAG with synthetic 25-mer oligonucleotides containing a single I lesion in single-stranded, mismatched, or single-nucleotide bulge contexts. We found that AAG has the highest catalytic efficiency toward a lesion that is presented in a single-nucleotide bulge. In contrast, AAG has more than 2000-fold reduced catalytic efficiency toward a single-stranded I-containing oligonucleotide relative to the duplexes. We have observed 20-fold differences in catalytic efficiency for the excision of the presumed biological target (paired with T) relative to alternative pairings such as C that might be formed by the replication of an unrepaired I. Furthermore, a linear free-energy relationship shows a strong inverse correlation between duplex stability and catalytic efficiency (slope = -0.6 to -1.0), indicating that gaining access to the base lesion provides a substantial barrier to AAG-catalyzed initiation of DNA repair. The observation that AAG recognizes a single-nucleotide bulge as efficiently as a mismatch implies that the recognition of DNA damage is remarkably plastic.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.