{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,23]],"date-time":"2026-02-23T18:31:31Z","timestamp":1771871491733,"version":"3.50.1"},"reference-count":56,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2014,1,21]],"date-time":"2014-01-21T00:00:00Z","timestamp":1390262400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-sa\/3.0\/"},{"start":{"date-parts":[[2014,2,28]],"date-time":"2014-02-28T00:00:00Z","timestamp":1393545600000},"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":["mBio"],"published-print":{"date-parts":[[2014,2,28]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The twin-arginine translocation (Tat) system, needed to transport folded proteins across biological membranes, has not been characterized in the gastric pathogen\n            <jats:named-content content-type=\"genus-species\">Helicobacter pylori<\/jats:named-content>\n            . Analysis of all\n            <jats:named-content content-type=\"genus-species\">H. pylori<\/jats:named-content>\n            genome sequences available thus far reveals the presence of single copies of\n            <jats:italic>tatA<\/jats:italic>\n            ,\n            <jats:italic>tatB<\/jats:italic>\n            , and\n            <jats:italic>tatC<\/jats:italic>\n            needed for the synthesis of a fully functional Tat system. Based on the presence of the twin-arginine hallmark in their signal sequence, only four\n            <jats:named-content content-type=\"genus-species\">H. pylori<\/jats:named-content>\n            proteins appear to be Tat dependent: hydrogenase (HydA), catalase-associated protein (KapA), biotin sulfoxide reductase (BisC), and the ubiquinol cytochrome oxidoreductase Rieske protein (FbcF). In the present study, targeted mutations were aimed at\n            <jats:italic>tatA<\/jats:italic>\n            ,\n            <jats:italic>tatB<\/jats:italic>\n            ,\n            <jats:italic>tatC<\/jats:italic>\n            , or\n            <jats:italic>queA<\/jats:italic>\n            (downstream gene control). While double homologous recombination mutations in\n            <jats:italic>tatB<\/jats:italic>\n            and\n            <jats:italic>queA<\/jats:italic>\n            were easily obtained, attempts at disrupting\n            <jats:italic>tatA<\/jats:italic>\n            proved unsuccessful, while deletion of\n            <jats:italic>tatC<\/jats:italic>\n            led to partial mutants following single homologous recombination, with cells retaining a chromosomal copy of\n            <jats:italic>tatC<\/jats:italic>\n            . Double homologous recombination\n            <jats:italic>tatC<\/jats:italic>\n            mutants were obtained only when a plasmid-borne, isopropyl-\u03b2-\n            <jats:sc>d<\/jats:sc>\n            -thiogalactopyranoside (IPTG)-inducible copy of\n            <jats:italic>tatC<\/jats:italic>\n            was introduced prior to transformation. These conditional\n            <jats:italic>tatC<\/jats:italic>\n            mutants could grow only in the presence of IPTG, suggesting that\n            <jats:italic>tatC<\/jats:italic>\n            is essential in\n            <jats:named-content content-type=\"genus-species\">H. pylori<\/jats:named-content>\n            .\n            <jats:italic>tatB<\/jats:italic>\n            and\n            <jats:italic>tatC<\/jats:italic>\n            mutants had lower hydrogenase and catalase activities than the wild-type strain did, and the ability of\n            <jats:italic>tatC<\/jats:italic>\n            mutants to colonize mouse stomachs was severely affected compared to the wild type. Chromosomal complementation of\n            <jats:italic>tatC<\/jats:italic>\n            mutants restored hydrogenase and catalase activities to wild-type levels, and additional expression of\n            <jats:italic>tatC<\/jats:italic>\n            in wild-type cells resulted in elevated Tat-dependent enzyme activities. Unexpectedly, the\n            <jats:italic>tat<\/jats:italic>\n            strains had cell envelope defects.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            This work reports the first characterization of the twin-arginine translocation (Tat) system in the gastric pathogen\n            <jats:named-content content-type=\"genus-species\">Helicobacter pylori<\/jats:named-content>\n            . While\n            <jats:italic>tatB<\/jats:italic>\n            mutants were easily obtained, only single-crossover partial\n            <jats:italic>tatC<\/jats:italic>\n            mutants or conditional\n            <jats:italic>tatC<\/jats:italic>\n            mutants could be generated, indicating that\n            <jats:italic>tatC<\/jats:italic>\n            is essential in\n            <jats:named-content content-type=\"genus-species\">H. pylori<\/jats:named-content>\n            , a surprising finding given the fact that only four proteins are predicted to be translocated by the Tat system in this bacterium. The levels of activity of hydrogenase and catalase, two of the predicted Tat-dependent enzymes, were affected in these mutants. In addition, all\n            <jats:italic>tat<\/jats:italic>\n            mutants displayed cell envelope defects, and\n            <jats:italic>tatC<\/jats:italic>\n            mutants were deficient in mouse colonization.\n          <\/jats:p>","DOI":"10.1128\/mbio.01016-13","type":"journal-article","created":{"date-parts":[[2014,1,22]],"date-time":"2014-01-22T05:34:53Z","timestamp":1390368893000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":20,"title":["Twin-Arginine Translocation System in Helicobacter pylori: TatC, but Not TatB, Is Essential for Viability"],"prefix":"10.1128","volume":"5","author":[{"given":"St\u00e9phane L.","family":"Benoit","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Georgia, Athens, Georgia, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert J.","family":"Maier","sequence":"additional","affiliation":[{"name":"Department of 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