{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T14:56:52Z","timestamp":1781103412831,"version":"3.54.1"},"reference-count":39,"publisher":"National Academy of Sciences","issue":"35","license":[{"start":{"date-parts":[[2017,2,16]],"date-time":"2017-02-16T00:00:00Z","timestamp":1487203200000},"content-version":"vor","delay-in-days":184,"URL":"http:\/\/www.pnas.org\/preview_site\/misc\/userlicense.xhtml"}],"funder":[{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM102318"],"award-info":[{"award-number":["GM102318"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2016,8,30]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    Contact-dependent growth inhibition (CDI) systems produce toxins that inhibit competing bacteria and immunity proteins that protect against self-inhibition. The CDI toxin deployed by\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    536 is a nuclease that only cleaves transfer RNA (tRNA) molecules when bound to the biosynthetic enzyme\n                    <jats:italic>O<\/jats:italic>\n                    -acetylserine sulfhydrylase (CysK). Here, we present crystal structures of the activated CysK\/toxin binary complex and the neutralized CysK\/toxin\/immunity protein ternary complex. CysK significantly increases toxin thermostability and promotes its interaction with tRNA substrates. Collectively, our results indicate that CysK stabilizes the toxin fold, thereby organizing the nuclease active site for substrate recognition and catalysis. We propose that the\n                    <jats:italic>E. coli<\/jats:italic>\n                    536 toxin may need to unfold when transferred between bacteria and that its interaction with CysK could ensure reactivation after entry into target cells.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1607112113","type":"journal-article","created":{"date-parts":[[2016,8,16]],"date-time":"2016-08-16T22:00:34Z","timestamp":1471384834000},"page":"9792-9797","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":46,"title":["Unraveling the essential role of CysK in CDI toxin activation"],"prefix":"10.1073","volume":"113","author":[{"given":"Parker M.","family":"Johnson","sequence":"first","affiliation":[{"name":"Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christina M.","family":"Beck","sequence":"additional","affiliation":[{"name":"Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA 93106-9625;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert P.","family":"Morse","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fernando","family":"Garza-S\u00e1nchez","sequence":"additional","affiliation":[{"name":"Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA 93106-9625;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David A.","family":"Low","sequence":"additional","affiliation":[{"name":"Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA 93106-9625;"},{"name":"Biomolecular Science and Engineering Program, University of California, Santa Barbara, CA 93106-9625;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher S.","family":"Hayes","sequence":"additional","affiliation":[{"name":"Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA 93106-9625;"},{"name":"Biomolecular Science and Engineering Program, University of California, Santa Barbara, CA 93106-9625;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Celia W.","family":"Goulding","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697;"},{"name":"Department of Pharmaceutical Sciences, University of California, Irvine, CA 92697"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2016,8,16]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"3754","DOI":"10.1016\/j.jmb.2015.09.010","article-title":"Contact-dependent growth inhibition (CDI) and CdiB\/CdiA two-partner secretion proteins","volume":"427","author":"Willett JL","year":"2015","unstructured":"JL Willett, ZC Ruhe, CW Goulding, DA Low, CS Hayes, Contact-dependent growth inhibition (CDI) and CdiB\/CdiA two-partner secretion proteins. J Mol Biol 427, 3754\u20133765 (2015).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_2_2","first-page":"e00480","article-title":"Receptor polymorphism restricts contact-dependent growth inhibition to members of the same species","volume":"4","author":"Ruhe ZC","year":"2013","unstructured":"ZC Ruhe, AB Wallace, DA Low, CS Hayes, Receptor polymorphism restricts contact-dependent growth inhibition to members of the same species. MBio 4, e00480\u201313 (2013).","journal-title":"MBio"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1038\/nature09490","article-title":"A widespread family of polymorphic contact-dependent toxin delivery systems in bacteria","volume":"468","author":"Aoki SK","year":"2010","unstructured":"SK Aoki, , A widespread family of polymorphic contact-dependent toxin delivery systems in bacteria. Nature 468, 439\u2013442 (2010).","journal-title":"Nature"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1186\/1745-6150-7-18","article-title":"Polymorphic toxin systems: Comprehensive characterization of trafficking modes, processing, mechanisms of action, immunity and ecology using comparative genomics","volume":"7","author":"Zhang D","year":"2012","unstructured":"D Zhang, RF de Souza, V Anantharaman, LM Iyer, L Aravind, Polymorphic toxin systems: Comprehensive characterization of trafficking modes, processing, mechanisms of action, immunity and ecology using comparative genomics. Biol Direct 7, 18 (2012).","journal-title":"Biol Direct"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.str.2014.02.012","article-title":"CdiA from Enterobacter cloacae delivers a toxic ribosomal RNase into target bacteria","volume":"22","author":"Beck CM","year":"2014","unstructured":"CM Beck, , CdiA from Enterobacter cloacae delivers a toxic ribosomal RNase into target bacteria. Structure 22, 707\u2013718 (2014).","journal-title":"Structure"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"21480","DOI":"10.1073\/pnas.1216238110","article-title":"Structural basis of toxicity and immunity in contact-dependent growth inhibition (CDI) systems","volume":"109","author":"Morse RP","year":"2012","unstructured":"RP Morse, , Structural basis of toxicity and immunity in contact-dependent growth inhibition (CDI) systems. 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