ArticleThe Journal of biological chemistry2012
Characterization of the human SNM1A and SNM1B/Apollo DNA repair exonucleases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 54 citations in OpenAlex.
- A Data-Analysis Pipeline for High-Throughput Systematic Evolution of Ligands by Exponential Enrichment (HT-SELEX) in the Characterization of Telomeric Proteins.bioRxiv : the preprint server for biology · 2026Article
- Molecular basis for CSB stimulation of the SNM1A DNA repair nuclease.Research square · 2025Article
- SNM1A is crucial for efficient repair of complex DNA breaks in human cells.Nature communications · 2024Article
- Cell-active small molecule inhibitors validate the SNM1A DNA repair nuclease as a cancer target.Chemical science · 2024Article
- DNA-PK controls Apollo's access to leading-end telomeres.Nucleic acids research · 2024Article
- Telomeric i-motifs and C-strands inhibit parallel G-quadruplex extension by telomerase.Nucleic acids research · 2023Article
- Deploying solid-phase synthesis to access thymine-containing nucleoside analogs that inhibit DNA repair nuclease SNM1A.Organic & biomolecular chemistry · 2023Article
- Two-Step Validation Approach for Tools To Study the DNA Repair Enzyme SNM1A.Chembiochem : a European journal of chemical biology · 2023Article
- Article
- Structure and Function of SNM1 Family Nucleases.Advances in experimental medicine and biology · 2023Review
- Characterization of the SARS-CoV-2 ExoN (nsp14ExoN-nsp10) complex: implications for its role in viral genome stability and inhibitor identification.Nucleic acids research · 2022Article
- Structural and mechanistic insights into the Artemis endonuclease and strategies for its inhibition.Nucleic acids research · 2021Article
- A phosphate binding pocket is a key determinant of exo- versus endo-nucleolytic activity in the SNM1 nuclease family.Nucleic acids research · 2021Article
- Synthesis and evaluation of squaramide and thiosquaramide inhibitors of the DNA repair enzyme SNM1A.Bioorganic & medicinal chemistry · 2021Article
- Identification of Bioactive SNM1A Inhibitors.ACS omega · 2021Article
- Probing the Binding Requirements of Modified Nucleosides with the DNA Nuclease SNM1A.Molecules (Basel, Switzerland) · 2021Article
- The SNM1A DNA repair nuclease.DNA repair · 2020Review
- Structural analysis of the catalytic domain of Artemis endonuclease/SNM1C reveals distinct structural features.The Journal of biological chemistry · 2020Article
- A hydroxamic-acid-containing nucleoside inhibits DNA repair nuclease SNM1A.Organic & biomolecular chemistry · 2019Article
- Squaramide-Based 5'-Phosphate Replacements Bind to the DNA Repair Exonuclease SNM1A.ChemistrySelect · 2018Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Human SNM1A and SNM1B/Apollo have both been implicated in the repair of DNA interstrand cross-links (ICLs) by cellular studies, and SNM1B is also required for telomere protection. Here, we describe studies on the biochemical characterization of the SNM1A and SNM1B proteins. The results reveal some fundamental differences in the mechanisms of the two proteins. Both SNM1A and SNM1B digest double-stranded and single-stranded DNA with a 5'-to-3' directionality in a reaction that is stimulated by divalent cations, and both nucleases are inhibited by the zinc chelator o-phenanthroline. We find that SNM1A has greater affinity for single-stranded DNA over double-stranded DNA that is not observed with SNM1B. Although both proteins demonstrate a low level of processivity on low molecular weight DNA oligonucleotide substrates, when presented with high molecular weight DNA, SNM1A alone is rendered much more active, being capable of digesting kilobase-long stretches of DNA. Both proteins can digest past ICLs induced by the non-distorting minor groove cross-linking agent SJG-136, albeit with SNM1A showing a greater capacity to achieve this. This is consistent with the proposal that SNM1A and SNM1B might exhibit some redundancy in ICL repair. Together, our work establishes differences in the substrate selectivities of SNM1A and SNM1B that are likely to be relevant to their in vivo roles and which might be exploited in the development of selective inhibitors.
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