ArticleNucleic acids research2020
The full-length structure of Thermus scotoductus OLD defines the ATP hydrolysis properties and catalytic mechanism of Class 1 OLD family nucleases.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 37 citations in OpenAlex.
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- Phage homing endonuclease amplifies anti-defense genes to evade bacterial immunity.Nature communications · 2026Article
- Structural basis of Retron-Eco8-mediated antiphage defense.Nucleic acids research · 2026Article
- Cran1, member of a new class of OLD family ATPases, functions in cell cycle progression in an archaeon.EMBO reports · 2026Article
- The uncharacterizedmicroPublication biology · 2026Article
- OLD amputates the anticodon arm of tRNAs during P2-Lambda interference.Nucleic acids research · 2025Article
- Specificity and mechanism of tRNA cleavage by the AriB Toprim nuclease of the PARIS bacterial immune system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Structural basis of the RNA-mediated Retron-Eco2 oligomerization.Cell discovery · 2025Article
- A DNA nicking Class 1 OLD family nuclease mediates phage defense in Vibrio cholerae and is countered by a phage-encoded inhibitor.Nucleic acids research · 2025Article
- West African-South American pandemic Vibrio cholerae encodes multiple distinct phage defence systems.Nature microbiology · 2025Article
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- Molecular basis of Gabija anti-phage supramolecular assemblies.Nature structural & molecular biology · 2024Article
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- Structural and biochemical insights into the mechanism of the Gabija bacterial immunity system.Nature communications · 2024Article
- Viral proteins activate PARIS-mediated tRNA degradation and viral tRNAs rescue infection.bioRxiv : the preprint server for biology · 2024Article
- Architecture and infection-sensing mechanism of the bacterial PARIS defense system.bioRxiv : the preprint server for biology · 2024Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
OLD family nucleases contain an N-terminal ATPase domain and a C-terminal Toprim domain. Homologs segregate into two classes based on primary sequence length and the presence/absence of a unique UvrD/PcrA/Rep-like helicase gene immediately downstream in the genome. Although we previously defined the catalytic machinery controlling Class 2 nuclease cleavage, degenerate conservation of the C-termini between classes precludes pinpointing the analogous residues in Class 1 enzymes by sequence alignment alone. Our Class 2 structures also provide no information on ATPase domain architecture and ATP hydrolysis. Here we present the full-length structure of the Class 1 OLD nuclease from Thermus scotoductus (Ts) at 2.20 Å resolution, which reveals a dimerization domain inserted into an N-terminal ABC ATPase fold and a C-terminal Toprim domain. Structural homology with genome maintenance proteins identifies conserved residues responsible for Ts OLD ATPase activity. Ts OLD lacks the C-terminal helical domain present in Class 2 OLD homologs yet preserves the spatial organization of the nuclease active site, arguing that OLD proteins use a conserved catalytic mechanism for DNA cleavage. We also demonstrate that mutants perturbing ATP hydrolysis or DNA cleavage in vitro impair P2 OLD-mediated killing of recBC-Escherichia coli hosts, indicating that both the ATPase and nuclease activities are required for OLD function in vivo.
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