{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T22:36:05Z","timestamp":1790980565658,"version":"4.1.0"},"reference-count":61,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2016,6,15]],"date-time":"2016-06-15T00:00:00Z","timestamp":1465948800000},"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":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2016,6,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            <jats:named-content content-type=\"genus-species\">Agrobacterium tumefaciens<\/jats:named-content>\n            has a cluster of genes (Atu3178, Atu3179, and Atu3180) encoding an ABC-type transporter, here named\n            <jats:italic>troA<\/jats:italic>\n            ,\n            <jats:italic>troB<\/jats:italic>\n            , and\n            <jats:italic>troC<\/jats:italic>\n            , respectively, which is shown here to be a zinc-specific uptake system. Reverse transcription (RT)-PCR analysis confirmed that\n            <jats:italic>troA<\/jats:italic>\n            ,\n            <jats:italic>troB<\/jats:italic>\n            , and\n            <jats:italic>troC<\/jats:italic>\n            are cotranscribed, with\n            <jats:italic>troC<\/jats:italic>\n            as the first gene of the operon. The\n            <jats:italic>yciC<\/jats:italic>\n            (Atu3181) gene is transcribed in the opposite orientation to that of the\n            <jats:italic>troCBA<\/jats:italic>\n            operon and belongs to a metal-binding GTPase family. Expression of\n            <jats:italic>troCBA<\/jats:italic>\n            and\n            <jats:italic>yciC<\/jats:italic>\n            was inducible under zinc-limiting conditions and was controlled by the zinc uptake regulator, Zur. Compared to the wild type, the mutant strain lacking\n            <jats:italic>troC<\/jats:italic>\n            was hypersensitive to a metal chelator, EDTA, and the phenotype could be rescued by the addition of zinc, while the strain with a single\n            <jats:italic>yciC<\/jats:italic>\n            mutation showed no phenotype. However,\n            <jats:italic>yciC<\/jats:italic>\n            was important for survival under zinc limitation when either\n            <jats:italic>troC<\/jats:italic>\n            or\n            <jats:italic>zinT<\/jats:italic>\n            was inactivated. The periplasmic zinc-binding protein, ZinT, could not function when TroC was inactivated, suggesting that ZinT may interact with TroCBA in zinc uptake. Unlike many other bacteria, the ABC-type transporter ZnuABC was not the major zinc uptake system in\n            <jats:named-content content-type=\"genus-species\">A. tumefaciens<\/jats:named-content>\n            . However, the important role of\n            <jats:named-content content-type=\"genus-species\">A. tumefaciens<\/jats:named-content>\n            ZnuABC was revealed when TroCBA was impaired. The strain containing double mutations in the\n            <jats:italic>znuA<\/jats:italic>\n            and\n            <jats:italic>troC<\/jats:italic>\n            genes exhibited a growth defect in minimal medium.\n            <jats:named-content content-type=\"genus-species\">A. tumefaciens<\/jats:named-content>\n            requires cooperation of zinc uptake systems and zinc chaperones, including TroCBA, ZnuABC, ZinT, and YciC, for survival under a wide range of zinc-limiting conditions.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            Both host and pathogen battle over access to essential metals, including zinc. In low-zinc environments, physiological responses that make it possible to acquire enough zinc are important for bacterial survival and could determine the outcome of host-pathogen interactions.\n            <jats:named-content content-type=\"genus-species\">A. tumefaciens<\/jats:named-content>\n            was found to operate a novel pathway for zinc uptake in which ZinT functions in concert with the high-affinity zinc importer TroCBA.\n          <\/jats:p>","DOI":"10.1128\/aem.00299-16","type":"journal-article","created":{"date-parts":[[2016,4,9]],"date-time":"2016-04-09T03:40:19Z","timestamp":1460173219000},"page":"3503-3514","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":31,"title":["Agrobacterium tumefaciens Zur Regulates the High-Affinity Zinc Uptake System TroCBA and the Putative Metal Chaperone YciC, along with ZinT and ZnuABC, for Survival under Zinc-Limiting Conditions"],"prefix":"10.1128","volume":"82","author":[{"given":"Paweena","family":"Chaoprasid","sequence":"first","affiliation":[{"name":"Laboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thanittra","family":"Dokpikul","sequence":"additional","affiliation":[{"name":"Environmental Toxicology, Chulabhorn Graduate Institute, Lak Si, Bangkok, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jaruwan","family":"Johnrod","sequence":"additional","affiliation":[{"name":"Applied Biological Sciences, Chulabhorn Graduate Institute, Lak Si, Bangkok, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sirin","family":"Sirirakphaisarn","sequence":"additional","affiliation":[{"name":"Applied Biological Sciences, Chulabhorn Graduate Institute, Lak Si, Bangkok, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sumontha","family":"Nookabkaew","sequence":"additional","affiliation":[{"name":"Laboratory of Pharmacology, Chulabhorn Research Institute, Lak Si, Bangkok, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rojana","family":"Sukchawalit","sequence":"additional","affiliation":[{"name":"Laboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok, Thailand"},{"name":"Applied Biological Sciences, Chulabhorn Graduate Institute, Lak Si, Bangkok, Thailand"},{"name":"Center of Excellence on Environmental Health and Toxicology (EHT), Ministry of Education, Bangkok, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Skorn","family":"Mongkolsuk","sequence":"additional","affiliation":[{"name":"Laboratory of Biotechnology, Chulabhorn Research Institute, Lak Si, Bangkok, Thailand"},{"name":"Center of Excellence on Environmental Health and Toxicology (EHT), Ministry of Education, Bangkok, Thailand"},{"name":"Department of Biotechnology, Faculty of Science, Mahidol University, Bangkok, Thailand"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.1993.73.1.79"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00775-008-0404-5"},{"key":"e_1_3_3_4_2","first-page":"967","article-title":"Succinate- and NADH oxidase systems of Escherichia coli membrane vesicles. 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