ArticleNucleic acids research2015
The structures of the SNM1A and SNM1B/Apollo nuclease domains reveal a potential basis for their distinct DNA processing activities.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 39 citations in OpenAlex.
- Precision medicine for atherosclerotic cardiovascular disease: Integrative genomics maps risk loci and AI-predicted functional consequences.Clinical and translational medicine · 2026Article
- Molecular basis for CSB stimulation of the SNM1A DNA repair nuclease.Research square · 2025Article
- DCLRE1B as a novel prognostic biomarker associated with immune infiltration: a pancancer analysis.Scientific reports · 2024Article
- DdrC, a unique DNA repair factor from D. radiodurans, senses and stabilizes DNA breaks through a novel lesion-recognition mechanism.Nucleic acids research · 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
- 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
- Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms.Cells · 2023Review
- Structure and Function of SNM1 Family Nucleases.Advances in experimental medicine and biology · 2023Review
- Inherited human Apollo deficiency causes severe bone marrow failure and developmental defects.Blood · 2022Article
- A phosphate binding pocket is a key determinant of exo- versus endo-nucleolytic activity in the SNM1 nuclease family.Nucleic acids research · 2021Article
- Structural and mechanistic insights into the Artemis endonuclease and strategies for its inhibition.Nucleic acids research · 2021Article
- Synthesis and evaluation of squaramide and thiosquaramide inhibitors of the DNA repair enzyme SNM1A.Bioorganic & medicinal chemistry · 2021Article
- Staring at the Naked Goddess: Unraveling the Structure and Reactivity of Artemis Endonuclease Interacting with a DNA Double Strand.Molecules (Basel, Switzerland) · 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
- Evolutionary insights into the active-site structures of the metallo-β-lactamase superfamily from a classification study with support vector machine.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- 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
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The human SNM1A and SNM1B/Apollo proteins are members of an extended family of eukaryotic nuclease containing a motif related to the prokaryotic metallo-β-lactamase (MBL) fold. SNM1A is a key exonuclease during replication-dependent and transcription-coupled interstrand crosslink repair, while SNM1B/Apollo is required for maintaining telomeric overhangs. Here, we report the crystal structures of SNM1A and SNM1B at 2.16 Å. While both proteins contain a typical MBL-β-CASP domain, a region of positive charge surrounds the active site of SNM1A, which is absent in SNM1B and explains the greater apparent processivity of SNM1A. The structures of both proteins also reveal a putative, wide DNA-binding groove. Extensive mutagenesis of this groove, coupled with detailed biochemical analysis, identified residues that did not impact on SNM1A catalytic activity, but drastically reduced its processivity. Moreover, we identified a key role for this groove for efficient digestion past DNA interstrand crosslinks, facilitating the key DNA repair reaction catalysed by SNM1A. Together, the architecture and dimensions of this groove, coupled to the surrounding region of high positive charge, explain the remarkable ability of SNM1A to accommodate and efficiently digest highly distorted DNA substrates, such as those containing DNA lesions.
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