{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T18:53:40Z","timestamp":1790189620588,"version":"4.1.0"},"reference-count":60,"publisher":"American Society for Microbiology","issue":"21","license":[{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2014,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    The mechanisms involved in the virulence of\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Yersinia pestis<\/jats:named-content>\n                    , the plague pathogen, are not fully understood. In previous research, we found that a\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Y. pestis<\/jats:named-content>\n                    mutant lacking the HicB3 (YPO3369) putative orphan antitoxin was attenuated for virulence in a murine model of bubonic plague. Toxin-antitoxin systems (TASs) are widespread in prokaryotes. Most bacterial species possess many TASs of several types. In type II TASs, the toxin protein is bound and neutralized by its cognate antitoxin protein in the cytoplasm. Here we identify the\n                    <jats:italic>hicA3<\/jats:italic>\n                    gene encoding the toxin neutralized by HicB3 and show that HicA3-HicB3 constitutes a new functional type II TAS in\n                    <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Y. pestis<\/jats:named-content>\n                    . Using biochemical and mutagenesis-based approaches, we demonstrate that the HicA3 toxin is an RNase with a catalytic histidine residue. HicB3 has two functions: it sequesters and neutralizes HicA3 by blocking its active site, and it represses transcription of the\n                    <jats:italic>hicA3B3<\/jats:italic>\n                    operon. Gel shift assays and reporter fusion experiments indicate that the HicB3 antitoxin binds to two operators in the\n                    <jats:italic>hicA3B3<\/jats:italic>\n                    promoter region. We solved the X-ray structures of HicB3 and the HicA3-HicB3 complex; thus, we present the first crystal structure of a TA complex from the HicAB family. HicB3 forms a tetramer that can bind two HicA3 toxin molecules. HicA3 is monomeric and folds as a double-stranded-RNA-binding domain. The HicB3 N-terminal domain occludes the HicA3 active site, whereas its C-terminal domain folds as a ribbon-helix-helix DNA-binding motif.\n                  <\/jats:p>","DOI":"10.1128\/jb.01932-14","type":"journal-article","created":{"date-parts":[[2014,8,12]],"date-time":"2014-08-12T02:35:47Z","timestamp":1407810947000},"page":"3712-3723","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":33,"title":["Functional and Structural Analysis of HicA3-HicB3, a Novel Toxin-Antitoxin System of Yersinia pestis"],"prefix":"10.1128","volume":"196","author":[{"given":"Sabrina","family":"Bibi-Triki","sequence":"first","affiliation":[{"name":"Equipe Peste et Yersinia pestis, INSERM U1019, Lille, France"},{"name":"CNRS UMR 8204, Lille, France"},{"name":"Institut Pasteur de Lille, Centre d'Infection et d'Immunit\u00e9, Lille, France"},{"name":"Universit\u00e9 Lille Nord de France, Lille, France"},{"name":"UDSL, Lille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"In\u00e8s","family":"Li de la Sierra-Gallay","sequence":"additional","affiliation":[{"name":"Equipe Fonction et Architecture des Assemblages MacroMol\u00e9culaires, IBBMC, Universit\u00e9 Paris-Sud, CNRS UMR 8619, Orsay, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noureddine","family":"Lazar","sequence":"additional","affiliation":[{"name":"Equipe Fonction et Architecture des Assemblages MacroMol\u00e9culaires, IBBMC, Universit\u00e9 Paris-Sud, CNRS UMR 8619, Orsay, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arnaud","family":"Leroy","sequence":"additional","affiliation":[{"name":"EA 4529, UFR de Pharmacie, Universit\u00e9 Paris-Sud, Ch\u00e2tenay-Malabry, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Herman","family":"Van Tilbeurgh","sequence":"additional","affiliation":[{"name":"Equipe Fonction et Architecture des Assemblages MacroMol\u00e9culaires, IBBMC, Universit\u00e9 Paris-Sud, CNRS UMR 8619, Orsay, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florent","family":"Sebbane","sequence":"additional","affiliation":[{"name":"Equipe Peste et Yersinia pestis, INSERM U1019, Lille, France"},{"name":"CNRS UMR 8204, Lille, France"},{"name":"Institut Pasteur de Lille, Centre d'Infection et d'Immunit\u00e9, Lille, France"},{"name":"Universit\u00e9 Lille Nord de France, Lille, France"},{"name":"UDSL, Lille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth","family":"Pradel","sequence":"additional","affiliation":[{"name":"Equipe Peste et Yersinia pestis, INSERM U1019, Lille, France"},{"name":"CNRS UMR 8204, Lille, France"},{"name":"Institut Pasteur de Lille, Centre d'Infection et d'Immunit\u00e9, Lille, France"},{"name":"Universit\u00e9 Lille Nord de France, Lille, France"},{"name":"UDSL, Lille, 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