ArticleThe Journal of biological chemistry2016
Scabin, a Novel DNA-acting ADP-ribosyltransferase from Streptomyces scabies.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 56 citations in OpenAlex.
- Description ofInternational journal of systematic and evolutionary microbiology · 2026Article
- Ancestral neuronal receptors are bacterial accessory toxins.Nature communications · 2026Article
- ADP-Ribosylation of Cytidine: A Novel Nucleic Acid Modification Reversed by NADAR Hydrolases.Toxins · 2026Article
- A survey of ADP-ribosyltransferase families in the pathogenic Legionella.BMC genomics · 2025Article
- Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin.Nature communications · 2024Article
- General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase-Substrate Complexes.Toxins · 2024Review
- A PL1 family pectate lyaseFrontiers in microbiology · 2024Article
- Proteomics fingerprinting reveals importance of iron and oxidative stress inFrontiers in microbiology · 2024Article
- Genomes of four Streptomyces strains reveal insights into putative new species and pathogenicity of scab-causing organisms.BMC genomics · 2023Article
- The DarT/DarG Toxin-Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies.Pathogens (Basel, Switzerland) · 2023Article
- Mammalian N1-adenosine PARylation is a reversible DNA modification.Nature communications · 2022Article
- Apprehending the NADViruses · 2022Article
- Crystal structures of pertussis toxin with NADThe Journal of biological chemistry · 2022Article
- Tracking of Diversity and Evolution in the Brown Rot FungiFrontiers in microbiology · 2022Article
- Functional roles of ADP-ribosylation writers, readers and erasers.Frontiers in cell and developmental biology · 2022Review
- A Structural Approach to Anti-Virulence: A Discovery Pipeline.Microorganisms · 2021Article
- Computational Structural Genomics Unravels Common Folds and Novel Families in the Secretome of Fungal PhytopathogenMolecular plant-microbe interactions : MPMI · 2021Article
- ADP-ribosylation of DNA and RNA.DNA repair · 2021Review
- ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function.Nucleic acids research · 2021Review
- The Buzz about ADP-Ribosylation Toxins fromToxins · 2021Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A bioinformatics strategy was used to identify Scabin, a novel DNA-targeting enzyme from the plant pathogen 87.22 strain of Streptomyces scabies Scabin shares nearly 40% sequence identity with the Pierisin family of mono-ADP-ribosyltransferase toxins. Scabin was purified to homogeneity as a 22-kDa single-domain enzyme and was shown to possess high NAD(+)-glycohydrolase (Km (NAD) = 68 ± 3 μm; kcat = 94 ± 2 min(-1)) activity with an RSQXE motif; it was also shown to target deoxyguanosine and showed sigmoidal enzyme kinetics (K0.5(deoxyguanosine) = 302 ± 12 μm; kcat = 14 min(-1)). Mass spectrometry analysis revealed that Scabin labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA. Several small molecule inhibitors were identified, and the most potent compounds were found to inhibit the enzyme activity with Ki values ranging from 3 to 24 μm PJ34, a well known inhibitor of poly-ADP-ribosyltransferases, was shown to be the most potent inhibitor of Scabin. Scabin was crystallized, representing the first structure of a DNA-targeting mono-ADP-ribosyltransferase enzyme; the structures of the apo-form (1.45 Å) and with two inhibitors (P6-E, 1.4 Å; PJ34, 1.6 Å) were solved. These x-ray structures are also the first high resolution structures of the Pierisin subgroup of the mono-ADP-ribosyltransferase toxin family. A model of Scabin with its DNA substrate is also proposed.
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