{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T12:52:51Z","timestamp":1791550371506,"version":"4.3.4"},"reference-count":33,"publisher":"Portland Press Ltd.","issue":"1","license":[{"start":{"date-parts":[[2019,7,25]],"date-time":"2019-07-25T00:00:00Z","timestamp":1564012800000},"content-version":"vor","delay-in-days":2736,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/2.5\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2012,2,15]]},"abstract":"<jats:p>DinG (damage inducible gene G) is a bacterial superfamily 2 helicase with 5\u2032\u21923\u2032 polarity. DinG is related to the XPD (xeroderma pigmentosum complementation group D) helicase family, and they have in common an FeS (iron\u2013sulfur)-binding domain that is essential for the helicase activity. In the bacilli and clostridia, the DinG helicase has become fused with an N-terminal domain that is predicted to be an exonuclease. In the present paper we show that the DinG protein from Staphylococcus aureus lacks an FeS domain and is not a DNA helicase, although it retains DNA-dependent ATP hydrolysis activity. Instead, the enzyme is an active 3\u2032\u21925\u2032 exonuclease acting on single-stranded DNA and RNA substrates. The nuclease activity can be modulated by mutation of the ATP-binding cleft of the helicase domain, and is inhibited by ATP or ADP, suggesting a modified role for the inactive helicase domain in the control of the nuclease activity. By degrading rather than displacing RNA or DNA strands, the S. aureus DinG nuclease may accomplish the same function as the canonical DinG helicase.<\/jats:p>","DOI":"10.1042\/bj20111903","type":"journal-article","created":{"date-parts":[[2011,12,15]],"date-time":"2011-12-15T09:34:56Z","timestamp":1323941696000},"page":"77-84","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["<i>Staphylococcus aureus<\/i> DinG, a helicase that has evolved into a nuclease"],"prefix":"10.1042","volume":"442","author":[{"given":"Anne-Marie","family":"McRobbie","sequence":"first","affiliation":[{"name":"Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bjoern","family":"Meyer","sequence":"additional","affiliation":[{"name":"Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christophe","family":"Rouillon","sequence":"additional","affiliation":[{"name":"Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Biljana","family":"Petrovic-Stojanovska","sequence":"additional","affiliation":[{"name":"Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huanting","family":"Liu","sequence":"additional","affiliation":[{"name":"Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Malcolm F.","family":"White","sequence":"additional","affiliation":[{"name":"Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2012,1,27]]},"reference":[{"key":"2021112217272601700_B1","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1146\/annurev.biochem.76.052305.115300","article-title":"Structure and mechanism of helicases and nucleic acid translocases","volume":"76","author":"Singleton","year":"2007","journal-title":"Annu. 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