{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:43:26Z","timestamp":1790729006440,"version":"4.1.0"},"reference-count":53,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2006,4,1]],"date-time":"2006-04-01T00:00:00Z","timestamp":1143849600000},"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":[[2006,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The biosynthesis of the \u03b2-lactam antibiotic penicillin in the filamentous fungus\n            <jats:italic>Aspergillus nidulans<\/jats:italic>\n            is catalyzed by three enzymes that are encoded by the\n            <jats:italic>acvA<\/jats:italic>\n            ,\n            <jats:italic>ipnA<\/jats:italic>\n            , and\n            <jats:italic>aatA<\/jats:italic>\n            genes. A variety of\n            <jats:italic>cis<\/jats:italic>\n            -acting DNA elements and regulatory factors form a complex regulatory network controlling these \u03b2-lactam biosynthesis genes. Regulators involved include the CCAAT-binding complex AnCF and AnBH1. AnBH1 acts as a repressor of the penicillin biosynthesis gene\n            <jats:italic>aatA<\/jats:italic>\n            . Until now, however, little information has been available on the signal transduction cascades leading to the transcription factors. Here we show that inhibition of protein kinase C (Pkc) activity in\n            <jats:italic>A. nidulans<\/jats:italic>\n            led to cytoplasmic localization of an AnBH1-enhanced green fluorescent protein (EGFP) fusion protein. Computer analysis of the genome and screening of an\n            <jats:italic>A. nidulans<\/jats:italic>\n            gene library revealed that the fungus possesses two putative Pkc-encoding genes, which we designated\n            <jats:italic>pkcA<\/jats:italic>\n            and\n            <jats:italic>pkcB<\/jats:italic>\n            . Only PkcA showed all the characteristic features of fungal Pkc's. Production of\n            <jats:italic>pkcA<\/jats:italic>\n            antisense RNA in\n            <jats:italic>A. nidulans<\/jats:italic>\n            led to reduced growth and conidiation in\n            <jats:italic>Aspergillus<\/jats:italic>\n            minimal medium, while in fermentation medium it led to enhanced expression of an\n            <jats:italic>aatAp-lacZ<\/jats:italic>\n            gene fusion, reduced pencillin production, and predominantly cytoplasmic localization of AnBH1. These data agree with the finding that inhibition of Pkc activity prevented nuclear localization of AnBH1-EGFP. As a result, repression of\n            <jats:italic>aatA<\/jats:italic>\n            expression was relieved. The involvement of Pkc in penicillin biosynthesis is also interesting in light of the fact that in the yeast\n            <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n            , Pkc plays a major role in maintaining cell integrity.\n          <\/jats:p>","DOI":"10.1128\/aem.72.4.2957-2970.2006","type":"journal-article","created":{"date-parts":[[2006,4,6]],"date-time":"2006-04-06T13:43:49Z","timestamp":1144331029000},"page":"2957-2970","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":47,"title":["Protein Kinase C (PkcA) of\n            <i>Aspergillus nidulans<\/i>\n            Is Involved in Penicillin Production"],"prefix":"10.1128","volume":"72","author":[{"given":"Martina","family":"Herrmann","sequence":"first","affiliation":[{"name":"Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology (HKI), and Department of Microbiology and Molecular Biology, Friedrich-Schiller-University Jena, Beutenbergstrasse 11a, D-07745 Jena, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Petra","family":"Spro\u0308te","sequence":"additional","affiliation":[{"name":"Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology (HKI), and Department of Microbiology and Molecular Biology, Friedrich-Schiller-University Jena, Beutenbergstrasse 11a, D-07745 Jena, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Axel A.","family":"Brakhage","sequence":"additional","affiliation":[{"name":"Department of Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology (HKI), and Department of Microbiology and Molecular Biology, Friedrich-Schiller-University Jena, Beutenbergstrasse 11a, D-07745 Jena, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1993.tb18038.x"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.2000.tb09204.x"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.112.20.3569"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1007\/s004380051089"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1992.tb17219.x"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(85)90187-8"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.66.10.4579-4581.2000"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/MMBR.62.3.547-585.1998"},{"key":"e_1_3_2_11_2","first-page":"159","volume":"4","year":"1999","unstructured":"Brakhage, A. 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