{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T13:51:13Z","timestamp":1791121873203,"version":"4.1.0"},"reference-count":40,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2001,2,1]],"date-time":"2001-02-01T00:00:00Z","timestamp":980985600000},"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":[[2001,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The biosynthetic genes\n            <jats:italic>pchDCBA<\/jats:italic>\n            and\n            <jats:italic>pchEF<\/jats:italic>\n            , which are known to be required for the formation of the siderophore pyochelin and its precursors salicylate and dihydroaeruginoate (Dha), are clustered with the\n            <jats:italic>pchR<\/jats:italic>\n            regulatory gene on the chromosome of\n            <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n            . The 4.6-kb region located downstream of the\n            <jats:italic>pchEF<\/jats:italic>\n            genes was found to contain three additional, contiguous genes,\n            <jats:italic>pchG<\/jats:italic>\n            ,\n            <jats:italic>pchH<\/jats:italic>\n            , and\n            <jats:italic>pchI<\/jats:italic>\n            , probably forming a\n            <jats:italic>pchEFGHI<\/jats:italic>\n            operon. The deduced amino acid sequences of PchH and PchI are similar to those of ATP binding cassette transport proteins with an export function. PchG is a homolog of the\n            <jats:italic>Yersinia pestis<\/jats:italic>\n            and\n            <jats:italic>Y. enterocolitica<\/jats:italic>\n            proteins YbtU and Irp3, which are involved in the biosynthesis of yersiniabactin. A null mutation in\n            <jats:italic>pchG<\/jats:italic>\n            abolished pyochelin formation, whereas mutations in\n            <jats:italic>pchH<\/jats:italic>\n            and\n            <jats:italic>pchI<\/jats:italic>\n            did not affect the amounts of salicylate, Dha, and pyochelin produced. The pyochelin biosynthetic genes were expressed from a vector promoter, uncoupling them from Fur-mediated repression by iron and PchR-dependent induction by pyochelin. In a\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            mutant lacking the entire pyochelin biosynthetic gene cluster, the expressed\n            <jats:italic>pchDCBA<\/jats:italic>\n            and\n            <jats:italic>pchEFG<\/jats:italic>\n            genes were sufficient for salicylate, Dha, and pyochelin production. Pyochelin formation was also obtained in the heterologous host\n            <jats:italic>Escherichia coli<\/jats:italic>\n            expressing\n            <jats:italic>pchDCBA<\/jats:italic>\n            and\n            <jats:italic>pchEFG<\/jats:italic>\n            together with the\n            <jats:italic>E. coli entD<\/jats:italic>\n            gene, which provides a phosphopantetheinyl transferase necessary for PchE and PchF activation. The PchG protein was purified and used in combination with PchD and phosphopantetheinylated PchE and PchF in vitro to produce pyochelin from salicylate,\n            <jats:sc>l<\/jats:sc>\n            -cysteine, ATP, NADPH, and\n            <jats:italic>S<\/jats:italic>\n            -adenosylmethionine. Based on this assay, a reductase function was attributed to PchG. In summary, this study completes the identification of the biosynthetic genes required for pyochelin formation from chorismate in\n            <jats:italic>P. aeruginosa<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/jb.183.3.813-820.2001","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:01:09Z","timestamp":1027764069000},"page":"813-820","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":136,"title":["Essential PchG-Dependent Reduction in Pyochelin Biosynthesis of\n            <i>Pseudomonas aeruginosa<\/i>"],"prefix":"10.1128","volume":"183","author":[{"given":"Cornelia","family":"Reimmann","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Laboratoire de Biologie Microbienne, Universite\u0301 de Lausanne, CH-1015 Lausanne, Switzerland,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiten M.","family":"Patel","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 021152"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura","family":"Serino","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Laboratoire de Biologie Microbienne, Universite\u0301 de Lausanne, CH-1015 Lausanne, Switzerland,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mario","family":"Barone","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Laboratoire de Biologie Microbienne, Universite\u0301 de Lausanne, CH-1015 Lausanne, Switzerland,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher T.","family":"Walsh","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 021152"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dieter","family":"Haas","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Laboratoire de Biologie Microbienne, Universite\u0301 de Lausanne, CH-1015 Lausanne, Switzerland,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.176.2.307-319.1994"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"14073","DOI":"10.1073\/pnas.96.24.14073","article-title":"Global GacA-steered control of cyanide and exoprotease production in Pseudomonas fluorescens involves specific ribosome binding sites","volume":"96","author":"Blumer C.","year":"1999","unstructured":"Blumer C. 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