{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T05:29:46Z","timestamp":1791091786995,"version":"4.1.0"},"reference-count":34,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2000,4,1]],"date-time":"2000-04-01T00:00:00Z","timestamp":954547200000},"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":[[2000,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            A 5-kbp region upstream of the\n            <jats:italic>are-ben-cat<\/jats:italic>\n            genes was cloned from\n            <jats:italic>Acinetobacter<\/jats:italic>\n            sp. strain ADP1, extending the supraoperonic cluster of catabolic genes to 30 kbp. Four open reading frames,\n            <jats:italic>salA<\/jats:italic>\n            ,\n            <jats:italic>salR<\/jats:italic>\n            ,\n            <jats:italic>salE<\/jats:italic>\n            , and\n            <jats:italic>salD<\/jats:italic>\n            , were identified from the nucleotide sequence. Reverse transcription-PCR studies suggested that these open reading frames are organized into two convergent transcription units,\n            <jats:italic>salAR<\/jats:italic>\n            and\n            <jats:italic>salDE<\/jats:italic>\n            . The\n            <jats:italic>salE<\/jats:italic>\n            gene, encoding a protein of 239 residues, was ligated into expression vector pET5a. Its product, SalE, was shown to have esterase activity against short-chain alkyl esters of 4-nitrophenol but was also able to hydrolyze ethyl salicylate to ethanol and salicylic acid. A mutant of ADP1 with a Km\n            <jats:sup>r<\/jats:sup>\n            cassette introduced into\n            <jats:italic>salE<\/jats:italic>\n            had lost the ability to utilize only ethyl and methyl salicylates of the esters tested as sole carbon sources, and no esterase activity against ethyl salicylate could be detected in cell extracts. SalE was induced during growth on ethyl salicylate but not during growth on salicylate itself.\n            <jats:italic>salD<\/jats:italic>\n            encoded a protein of undetermined function with homologies to the\n            <jats:italic>Escherichia coli<\/jats:italic>\n            FadL membrane protein, which is involved in facilitating fatty acid transport, and a number of other proteins detected during aromatic catabolism, which may also function in hydrocarbon transport or uptake processes. A Km\n            <jats:sup>r<\/jats:sup>\n            cassette insertion in\n            <jats:italic>salD<\/jats:italic>\n            deleteriously affected cell growth and viability. The\n            <jats:italic>salA<\/jats:italic>\n            and\n            <jats:italic>salR<\/jats:italic>\n            gene products closely resemble two\n            <jats:italic>Pseudomonas<\/jats:italic>\n            proteins, NahG and NahR, respectively encoding salicylate hydroxylase and the LysR family regulator of both salicylate and naphthalene catabolism.\n            <jats:italic>salA<\/jats:italic>\n            was cloned into pUC18 together with\n            <jats:italic>salR<\/jats:italic>\n            and\n            <jats:italic>salE<\/jats:italic>\n            , and its gene product showed salicylate-inducible hydroxylase activity against a range of substituted salicylates, with the same relative specific activities as found in wild-type ADP1 grown on salicylate. Mutations involving insertion of Km\n            <jats:sup>r<\/jats:sup>\n            cassettes into\n            <jats:italic>salA<\/jats:italic>\n            and\n            <jats:italic>salR<\/jats:italic>\n            eliminated expression of salicylate hydroxylase activity and the ability to grow on either salicylate or ethyl salicylate. Studies of mutants with disruptions of genes of the \u03b2-ketoadipate pathway with or without an additional\n            <jats:italic>salE<\/jats:italic>\n            mutation confirmed that ethyl salicylate and salicylate were channeled into the \u03b2-ketoadipate pathway at the level of catechol and thence dissimilated by the\n            <jats:italic>cat<\/jats:italic>\n            gene products. SalR appeared to regulate expression of\n            <jats:italic>salA<\/jats:italic>\n            but not\n            <jats:italic>salE<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/jb.182.7.2018-2025.2000","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:01:09Z","timestamp":1027764069000},"page":"2018-2025","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":45,"title":["<i>sal<\/i>\n            Genes Determining the Catabolism of Salicylate Esters Are Part of a Supraoperonic Cluster of Catabolic Genes in\n            <i>Acinetobacter<\/i>\n            sp. 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