{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T04:18:23Z","timestamp":1779337103712,"version":"3.51.4"},"reference-count":51,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2021,1,13]],"date-time":"2021-01-13T00:00:00Z","timestamp":1610496000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["105440"],"award-info":[{"award-number":["105440"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Scabin is a mono-ADP-ribosyltransferase toxin\/enzyme and possible virulence factor produced by the agriculture pathogen, Streptomyces scabies. Recently, molecular dynamic approaches and MD simulations revealed its interaction with both NAD+ and DNA substrates. An Essential Dynamics Analysis identified a crab-claw-like mechanism, including coupled changes in the exposed motifs, and the R\u03b21-RLa-NLc-STT\u03b22-WPN-WARTT-(QxE)ARTT sequence motif was proposed as a catalytic signature of the Pierisin family of DNA-acting toxins. A new fluorescence assay was devised to measure the kinetics for both RNA and DNA substrates. Several protein variants were prepared to probe the Scabin-NAD-DNA molecular model and to reveal the reaction mechanism for the transfer of ADP-ribose to the guanine base in the DNA substrate. The results revealed that there are several lysine and arginine residues in Scabin that are important for binding the DNA substrate; also, key residues such as Asn110 in the mechanism of ADP-ribose transfer to the guanine base were identified. The DNA-binding residues are shared with ScARP from Streptomyces coelicolor but are not conserved with Pierisin-1, suggesting that the modification of guanine bases by ADP-ribosyltransferases is divergent even in the Pierisin family.<\/jats:p>","DOI":"10.3390\/toxins13010055","type":"journal-article","created":{"date-parts":[[2021,1,13]],"date-time":"2021-01-13T21:50:54Z","timestamp":1610574654000},"page":"55","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Mapping the DNA-Binding Motif of Scabin Toxin, a Guanine Modifying Enzyme from Streptomyces scabies"],"prefix":"10.3390","volume":"13","author":[{"given":"Maritza","family":"Vatta","sequence":"first","affiliation":[{"name":"Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bronwyn","family":"Lyons","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology and Center for Blood Research, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC V6T 1Z3, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kayla A.","family":"Heney","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, McGill University, Montreal, QC H3G 1Y6, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Taylor","family":"Lidster","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Brock University, St. Catherines, ON L2S 3A1, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8559-8384","authenticated-orcid":false,"given":"A. Rod","family":"Merrill","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,1,13]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1038\/nrmicro3310","article-title":"Novel bacterial ADP-ribosylating toxins: Structure and function","volume":"12","author":"Simon","year":"2014","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"10608","DOI":"10.1073\/pnas.96.19.10608","article-title":"Molecular cloning of an apoptosis-inducing protein, pierisin, from cabbage butterfly: Possible involvement of ADP-ribosylation in its activity","volume":"96","author":"Watanabe","year":"1999","journal-title":"Proc. Natl. Acad. Sci. 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