{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1390579830890111488.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.2323/jgam.2023.01.002"}},{"identifier":{"@type":"PMID","@value":"36805586"}},{"identifier":{"@type":"URI","@value":"https://www.jstage.jst.go.jp/article/jgam/69/3/69_2023.01.002/_pdf"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@language":"en","@value":"TrLys9 participates in fungal development and lysine biosynthesis in <i>Trichoderma reesei</i>"}],"dc:language":"en","description":[{"type":"abstract","notation":[{"@language":"en","@value":"<p>Fungi uniquely synthesize lysine through the α-aminoadipate pathway. The saccharopine reductase ScLys9 catalyzes the formation of saccharopine from ɑ-aminoadipate 6-semialdehyde, the seventh step in the lysine biosynthesis pathway in <i>Saccharomyces cerevisiae</i>. Here, we characterized the functions of TrLys9, an ortholog of <i>S. cerevisiae</i> ScLys9 in the industrial filamentous fungus <i>Trichoderma reesei</i>. Transcriptional level analysis indicated that <i>TrLYS9</i> expression was higher in the conidial stage than in other stages. Disruption of <i>TrLYS9</i> led to lysine auxotrophy. Phenotype analysis of the <i>ΔTrlys9</i> mutant showed that <i>TrLYS9 </i>was involved in fungal development including vegetative growth, conidiation, and conidial germination and lysine biosynthesis. Cellulase production was also impaired in the <i>ΔTrlys9</i> mutant due to the failure of conidial germination in liquid cellulase-inducing medium. Defects in radial growth and asexual development of the <i>ΔTrlys9</i> mutant were fully recovered when exogenous lysine was added to the medium. These results imply that TrLys9 is involved in fungal development and lysine biosynthesis in <i>T. reesei</i>.</p>"}],"abstractLicenseFlag":"disallow"}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1410579830890111488","@type":"Researcher","foaf:name":[{"@language":"en","@value":"Lan Jinling"}],"jpcoar:affiliationName":[{"@language":"en","@value":"College of Plant Protection, Jilin Agricultural University"},{"@language":"en","@value":"Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences"},{"@language":"en","@value":"National Center of Technology Innovation for Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences"}]},{"@id":"https://cir.nii.ac.jp/crid/1410579830890111490","@type":"Researcher","foaf:name":[{"@language":"en","@value":"Zhang  Lin"}],"jpcoar:affiliationName":[{"@language":"en","@value":"College of Plant Protection, Jilin Agricultural University"},{"@language":"en","@value":"Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences"},{"@language":"en","@value":"National Center of Technology Innovation for Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences"}]},{"@id":"https://cir.nii.ac.jp/crid/1410579830890111491","@type":"Researcher","foaf:name":[{"@language":"en","@value":"Gao Jie"}],"jpcoar:affiliationName":[{"@language":"en","@value":"College of Plant Protection, Jilin Agricultural University"}]},{"@id":"https://cir.nii.ac.jp/crid/1410579830890111489","@type":"Researcher","foaf:name":[{"@language":"en","@value":"He Ronglin"}],"jpcoar:affiliationName":[{"@language":"en","@value":"Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences"},{"@language":"en","@value":"National Center of Technology Innovation for Synthetic Biology, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00221260"},{"@type":"LISSN","@value":"00221260"},{"@type":"EISSN","@value":"13498037"}],"prism:publicationName":[{"@language":"en","@value":"The Journal of General and Applied Microbiology"},{"@language":"en","@value":"J. Gen. Appl. Microbiol."}],"dc:publisher":[{"@language":"en","@value":"Applied Microbiology, Molecular and Cellular Biosciences Research Foundation"},{"@language":"ja","@value":"公益財団法人　応用微生物学・分子細胞生物学研究奨励会"}],"prism:publicationDate":"2023","prism:volume":"69","prism:number":"3","prism:startingPage":"159","prism:endingPage":"166"},"reviewed":"false","url":[{"@id":"https://www.jstage.jst.go.jp/article/jgam/69/3/69_2023.01.002/_pdf"}],"availableAt":"2023","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=lysine%20biosynthesis","dc:title":"lysine biosynthesis"},{"@id":"https://cir.nii.ac.jp/all?q=%3Ci%3ETrichoderma%20reesei%3C/i%3E","dc:title":"<i>Trichoderma reesei</i>"},{"@id":"https://cir.nii.ac.jp/all?q=vegetative%20growth","dc:title":"vegetative growth"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360011143491075584","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Involvement of a<i>Magnaporthe grisea</i>Serine/Threonine Kinase Gene, Mg<i>ATG1</i>, in Appressorium Turgor and Pathogenesis"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016866569586176","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"pRS yeast vectors with a\n            <i>LYS2</i>\n            marker"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016866621122304","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The information highways of a biotechnological workhorse – signal transduction in Hypocrea jecorina"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016866687618304","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Amino acid biosynthetic pathways as antifungal targets for fungal infections"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016867531831936","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Connections Between Amino Acid Metabolisms in Plants: Lysine as an Example"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016868136425344","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Development of a new Agrobacterium-mediated transformation system based on a dual auxotrophic approach in the filamentous fungus Aspergillus oryzae"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016868295474944","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The MET13 Methylenetetrahydrofolate Reductase Gene Is Essential for Infection-Related Morphogenesis in the Rice Blast Fungus Magnaporthe oryzae"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016868327236608","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Long-term strain improvements accumulate mutations in regulatory elements responsible for hyper-production of cellulolytic enzymes"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016870079096064","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Methylenetetrahydrofolate Reductase Activity Is Involved in the Plasma Membrane Redox System Required for Pigment Biosynthesis in Filamentous Fungi"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292618984984832","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Development of highly efficient, low-cost lignocellulolytic enzyme systems in the post-genomic era"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292619187867008","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292620992895488","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Lysine biosynthesis and metabolism in fungi"}]},{"@id":"https://cir.nii.ac.jp/crid/1360298341295403136","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Histidine biosynthesis plays a crucial role in metal homeostasis and virulence of<i>Aspergillus fumigatus</i>"}]},{"@id":"https://cir.nii.ac.jp/crid/1360298343163814400","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Gene Targeting in<i>Penicillium chrysogenum</i>: Disruption of the<i>lys2</i>Gene Leads to Penicillin Overproduction"}]},{"@id":"https://cir.nii.ac.jp/crid/1360298345562817664","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Isopropylmalate isomerase MoLeu1 orchestrates leucine biosynthesis, fungal development, and pathogenicity in Magnaporthe oryzae"}]},{"@id":"https://cir.nii.ac.jp/crid/1360576122503478016","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A proteome-wide atlas of lysine-reactive 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biosynthesis gene lysF encoding homoaconitase leads to attenuated virulence in a low-dose mouse infection model of invasive aspergillosis"}]},{"@id":"https://cir.nii.ac.jp/crid/1360579820519695488","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Functional Genomics of Aspergillus oryzae: Strategies and Progress"}]},{"@id":"https://cir.nii.ac.jp/crid/1360845539021370240","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Catabolism of lysine in Penicillium chrysogenum leads to formation of 2-aminoadipic acid, a precursor of penicillin biosynthesis"}]},{"@id":"https://cir.nii.ac.jp/crid/1360855568442962176","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Overexpression of the lys1 gene in Penicillium chrysogenum : homocitrate synthase levels, α-aminoadipic acid pool and penicillin 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for infection-related morphogenesis and pathogenicity in the rice blast fungus Magnaporthe oryzae"}]},{"@id":"https://cir.nii.ac.jp/crid/1361137045548250496","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A Study of the Protein Secretory Pathway of Aspergillus niger Using a Glucoamylase–GFP Fusion Protein"}]},{"@id":"https://cir.nii.ac.jp/crid/1361981469993471232","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The α-Aminoadipate Pathway for Lysine Biosynthesis in Fungi"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544420923383936","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"HisB as novel selection marker for gene targeting approaches in Aspergillus niger"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107368477901952","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT 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