title: L-arginine is essential for conidiation in the filamentous fungus Coniothyrium minitans.
abstract: Conidiation is important in the life cycles of mitosporic fungi for survival and transmission. A full-length cDNA of one gene named CMCPS1 encoding L-arginine-specific carbamoyl-phosphate synthase was obtained from Coniothyrium minitans, a sclerotial parasite of the plant pathogenic fungus Sclerotinia sclerotiorum. T-DNA insertional disruption of CMCPS1 resulted in conidiation deficiency of mutant ZS-1T2029, and this was confirmed with the RNAi technique. The phenotype was restored by complementation with L-arginine, and the effect of L-arginine on conidiation may be mediated by nitric oxide, which is catalyzed by nitric oxide synthase (NOS). Conidiation of ZS-1T2029 was restored by sodium nitroprussiate, a NO donor; and conidiation of wild type strain ZS-1 could be suppressed by L-NAME, an inhibitor of NOS. The highest amount of NO in mycelia was detected at an early stage of conidiation (72 hpi) in liquid shake culture medium. Staining with the NO-sensitive fluorescent probe, DAF-FM DA, gave strong fluorescent signals in primordia and young pycnidia. This work presents the first report that L-arginine is involved in conidiation of C. minitans, and the possibility of L-arginine-derived nitric oxide-mediated conidiation among fungi and possible modes of action are discussed.
authors: The Key Lab of Plant Pathology of Hubei Province, College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, Hubei Province, PR China.
authors: Xiaoyan
authors: X
authors: Gong
authors: Yanping
authors: Y
authors: Fu
authors: Daohong
authors: D
authors: Jiang
authors: Guoqing
authors: G
authors: Li
authors: Xianhong
authors: X
authors: Yi
authors: Youliang
authors: Y
authors: Peng
mesh_terms: D001120:Arginine / Q000378:metabolism* / Q000494:pharmacology; D001203:Ascomycota / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D015139:Blotting, Southern; D019733:Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor / Q000235:genetics / Q000378:metabolism; D002956:Citrulline / Q000494:pharmacology; D004269:DNA, Bacterial / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D019331:NG-Nitroarginine Methyl Ester / Q000494:pharmacology; D020030:Nitric Oxide Donors / Q000494:pharmacology; D019001:Nitric Oxide Synthase / Q000037:antagonists & inhibitors / Q000378:metabolism; D009599:Nitroprusside / Q000494:pharmacology; D034622:RNA Interference; D015398:Signal Transduction / Q000187:drug effects / Q000235:genetics / Q000502:physiology; D013172:Spores, Fungal / Q000187:drug effects / Q000235:genetics / Q000254:growth & development*
chemical_list: D004269:DNA, Bacterial; D005656:Fungal Proteins; D020030:Nitric Oxide Donors; C036483:T-DNA; D009599:Nitroprusside; D002956:Citrulline; D001120:Arginine; D019001:Nitric Oxide Synthase; D019733:Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor; C064716:carbamoyl phosphate synthetase (arginine-specific); D019331:NG-Nitroarginine Methyl Ester