title: The distinctive regulatory roles of PrtT in the cell metabolism of Penicillium oxalicum.
abstract: PrtT is a fungal-specific transcription activator of extracellular proteases in Aspergilli. In this study, the roles of the PrtT homolog from Penicillum oxalicum was investigated by transcription profiling in combination with electrophoretic mobility shift assay (EMSA). The prtT deletion dramatically reduced extracellular protease activities and caused intracellular nutrient limitation when cultured on casein as the sole carbon source. PrtT was found to directly regulate the expression of an intracellular peptidase encoding gene (tripeptidyl-peptidase) and the gene encoding the extracellular dipeptidyl-aminopeptidase V, in addition to the expected extracellular peptidase genes (carboxypeptidase and aspergillopepsin). Five amylase genes (α-amylase, glucoamylase, α-glucosidase) and three major facilitator superfamily transporter genes related to maltose, monosaccharide and peptide transporting were also confirmed as putative targets of PrtT by EMSA. In contrast, the transcription levels of other genes encoding polysaccharide degrading enzymes (e.g. cellulases) and most iron or multidrug transporter encoding genes were up- or down-regulated in the ΔprtT mutant due to nutrient limitation resulting from the reduced usage of the sole carbon source, casein. These results deepen the understanding of the interaction of regulation systems for nitrogen and carbon catabolism, which benefit strain improvement of P. oxalicum for industrial enzyme production.
authors: Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China.
authors: Ling
authors: L
authors: Chen
authors: Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China.
authors: Gen
authors: G
authors: Zou
authors: Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China.
authors: Lei
authors: L
authors: Zhang
authors: Fungal Physiology Research Group, CBS-KNAW Fungal Biodiversity Centre, Uppsalalaan 8, 3584 CT, Utrecht, The Netherlands.
authors: Ronald P
authors: RP
authors: de Vries
authors: Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China.
authors: Xing
authors: X
authors: Yan
authors: Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China.
authors: Jun
authors: J
authors: Zhang
authors: Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China.
authors: Rui
authors: R
authors: Liu
authors: Key Laboratory of Insect Developmental and Evolutionary Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China.
authors: Chengshu
authors: C
authors: Wang
authors: State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong 250100, China.
authors: Yinbo
authors: Y
authors: Qu
authors: Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200032, China. Electronic address: zhouzhihua@sippe.ac.cn.
authors: Zhihua
authors: Z
authors: Zhou
mesh_terms: D000626:Aminopeptidases / Q000235:genetics / Q000378:metabolism; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal; D010407:Penicillium / Q000235:genetics / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism; D000516:alpha-Amylases / Q000235:genetics / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D000516:alpha-Amylases; D010447:Peptide Hydrolases; D000626:Aminopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C048001:tripeptidyl-peptidase 2; D012697:Serine Endopeptidases
keywords: Cell metabolism; Gene regulation; Nutrient limitation; Penicillium oxalicum; PrtT