title: Characterization of the oat1 gene of Penicillium chrysogenum encoding an omega-aminotransferase: induction by L-lysine, L-ornithine and L-arginine and repression by ammonium.
abstract: The Penicillium chrysogenum oat1 gene, which encodes a class III omega-aminotransferase, was cloned and characterized. This enzyme converts lysine into 2-aminoadipic semialdehyde, and plays an important role in the biosynthesis of 2-aminoadipic acid, a precursor of penicillin and other beta-lactam antibiotics. The enzyme is related to ornithine-5-aminotransferases and to the lysine-6-aminotransferases encoded by the lat genes found in bacterial cephamycin gene clusters. Expression of oat1 is induced by lysine, ornithine and arginine, and repressed by ammonium ions. AreA-binding GATA and GATT sequences involved in regulation by ammonium, and an 8-bp direct repeat associated with arginine induction in Emericella (Aspergillus nidulans and Saccharomyces cerevisiae, were found in the oat1 promoter region. Deletion of the oat1 gene resulted in the loss of omega-aminotransferase activity. The null mutants were unable to grow on ornithine or arginine as sole nitrogen sources and showed reduced growth on lysine. Complementation of the null mutant with the oat1 gene restored normal levels of omega-aminotransferase activity and the ability to grow on ornithine, arginine and lysine. The role of the oat1 gene in the biosynthesis of 2-aminoadipic acid is discussed.
authors.affiliation: Instituto de Biotecnología de León (INBIOTEC), Parque Científico de León, Spain.
authors.forename: Leopoldo
authors.initials: L
authors.lastname: Naranjo
authors.forename: Mònica
authors.initials: M
authors.lastname: Lamas-Maceiras
authors.forename: Ricardo V
authors.initials: RV
authors.lastname: Ullán
authors.forename: Sonia
authors.initials: S
authors.lastname: Campoy
authors.forename: Fernando
authors.initials: F
authors.lastname: Teijeira
authors.forename: Javier
authors.initials: J
authors.lastname: Casqueiro
authors.forename: Juan F
authors.initials: JF
authors.lastname: Martín
mesh_terms: D015074:2-Aminoadipic Acid / Q000096:biosynthesis*; D000595:Amino Acid Sequence; D001120:Arginine / Q000494:pharmacology; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D017124:Conserved Sequence / Q000235:genetics; D017931:DNA Primers; D018076:DNA, Complementary / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics; D017353:Gene Deletion; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects* / Q000235:genetics; D007438:Introns / Q000235:genetics; D008239:Lysine / Q000378:metabolism* / Q000494:pharmacology; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D009952:Ornithine / Q000494:pharmacology; D010408:Penicillium chrysogenum / Q000201:enzymology* / Q000254:growth & development; D011401:Promoter Regions, Genetic / Q000235:genetics; D000644:Quaternary Ammonium Compounds / Q000633:toxicity; D017422:Sequence Analysis, DNA; D000637:Transaminases / Q000235:genetics* / Q000378:metabolism*; D014157:Transcription Factors / Q000235:genetics
chemical_list: C079728:AreA protein, Aspergillus nidulans; D017931:DNA Primers; D018076:DNA, Complementary; D005656:Fungal Proteins; D000644:Quaternary Ammonium Compounds; D014157:Transcription Factors; D015074:2-Aminoadipic Acid; D001120:Arginine; D009952:Ornithine; D000637:Transaminases; D008239:Lysine