Pleurotus and Agrocybe hemolysins,new proteins hypothetically involved in fungal fruiting |
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| Institution: | 1. Department of Biology, Biotechnical Faculty, University of Ljubljana, Večna pot 111, 1000 Ljubljana, Slovenia;2. Department of Biochemistry and Molecular Biology, Jožef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia;3. Department of Wood Science and Technology, Biotechnical Faculty, University of Ljubljana, Rožna dolina, Cesta VIII/34, 1000 Ljubljana, Slovenia;1. Laboratory, Biological Business Department, Ichimasa Kamaboko Co., Ltd., 77-1 Junishin, Agano-shi, Niigata, 959-1936, Japan;2. Faculty of Agriculture, Tottori University, 4-101 Koyama-cho Minami, Tottori, 680-8553, Japan;3. Graduate School of Sustainability Science, Tottori University, 4-101 Koyama-cho Minami, Tottori, 680-8553, Japan;1. Institute of Geochemistry and Petrology, Department of Earth Sciences, ETH Zurich, Zurich, Switzerland;2. Earth Observatory of Singapore, Nanyang Technological University, Singapore;3. Sedimentology and Environmental Geology, University of Göttingen, Göttingen, Germany;4. Department of Earth Sciences, Uppsala University, Uppsala, Sweden;1. Unidad de Biofísica (CSIC, UPV/EHU), and Departamento de Bioquímica, Universidad del País Vasco, Aptdo. 644, 48080 Bilbao, Spain;2. OWL, Parque Tecnológico de Bizkaia, Bizkaia, Spain |
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| Abstract: | Novel hemolytic proteins, ostreolysin and aegerolysin, were purified from the fruiting bodies of the edible mushrooms Pleurotus ostreatus and Agrocybe aegerita. Both ostreolysin and aegerolysin have a molecular weight of about 16 kDa, have low isoelectric points of 5.0 and 4.85, are thermolabile, and hemolytic to bovine erythrocytes at nanomolar concentrations. Their activity is impaired by micromolar Hg2+ but not by membrane lipids and serum low-density lipoproteins (LDL). The sequence of respectively 50 and 10 N-terminal amino acid residues of ostreolysin and aegerolysin has been determined and found to be highly identical with a cDNA-derived amino acid sequence of putative Aa-Pri1 protein from the mushroom A. aegerita, Asp-hemolysin from Aspergillus fumigatus, and two bacterial hemolysin-like proteins expressed during sporulation. We found that ostreolysin is expressed during formation of primordia and fruiting bodies, which is in accord with previous finding that the Aa-Pri1 gene is specifically expressed during fruiting initiation. It is suggestive that the isolated hemolysins play an important role in initial phase of fungal fruiting. |
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