Identification of target amino acids that affect interactions of fungal polygalacturonases and their plant inhibitors |
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| Affiliation: | 1. Max-Planck-Institute of Chemical Ecology, Carl-Zeiss Promenade 10, D-07745, Jena, Germany;2. School of Biological Sciences, Washington State University, Vancouver, WA, 98686, U.S.A.;3. Complex Carbohydrate Research Center, University of Georgia, Athens, GA, 30602-4712, U.S.A.;4. Institute of Systematic Botany and Geobotany, Gregor-Mendel-Str. 33, A-1180, Vienna, Austria;5. Department of Pomology, University of California, Davis, CA, 95616, U.S.A.;1. Department of Surgery, Cantonal Hospital, St.Gallen, Switzerland;2. Institute of Medical Biometry and Informatics, University of Heidelberg, Germany;3. Department of Medical Oncology and Hematology, Cantonal Hospital, St.Gallen, Switzerland;4. Department of Visceral Surgery and Medicine, University of Berne, Switzerland;5. Department of Radiation Oncology, Cantonal Hospital, St.Gallen, Switzerland;1. Department of Agri-Food and Environmental Science, Università di Firenze, via delle Idee 30, 50019, Sesto Fiorentino, Italy;2. Department of Biology, Università di Firenze, via Micheli 1, 50121, Firenze, Italy;3. Department of Earth Science, Università di Firenze, via La Pira 4, 50121, Firenze, Italy;4. Department of Biomedical Experimental and Clinical Sciences, Università di Firenze, viale Morgagni 50, 50134, Firenze, Italy;1. Jiangmen Central Hospital Affiliated Jiangmen Hospital of Sun YAT-SEN University, Jiangmen, 529000, China;2. Department of Pharmacology, Wuhan University School of Basic Medical Sciences, Wuhan, 430071, China;3. Gansu provincial hospital of TCM Affiliated to Gansu University of Chinese Medicine, Gansu, 730050, China;4. Hubei Provincial Key Laboratory of Developmentally Originated Disease, Wuhan, 430071, China;1. IBS, Unit of Personality, Work and Health Psychology, University of Helsinki (Siltavuorenpenger 1 A), P.O.Box 9, 00014, Helsinki, Finland;2. Unit of Psychology, Faculty of Education, University of Oulu, Oulu, Finland;3. Helsinki Collegium for Advanced Studies, University of Helsinki, Helsinki, Finland;4. National Institute for Health and Welfare, Helsinki, Finland;5. Department of Clinical Chemistry, Fimlab Laboratories and School of Medicine, University of Tampere, Tampere, Finland;6. Department of Clinical Physiology, Turku University Hospital and Research Centre of Applied and Preventive Cardiovascular Medicine, University of Turku, Turku, Finland |
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| Abstract: | Plant polygalacturonase inhibitor proteins (PGIPs) bind fungal polygalacturonases (PGs), but inhibition specificities and kinetics vary within and among species. Purified bean PGIP inhibited all fungal PGs we tested, includingFusarium moniliforme PG. Pear PGIP, however, was only effective against Botrytis cinerea PG. Moreover, tomato PGIP inhibited B. cinerea PG more than Aspergillus niger PG. Models of codon evolution for 22 dicot PGIPs and 19 fungal PGs indicated that advantageous substitutions dominate the molecular evolution of these genes and identified 9 amino acid residues, each, that are likely to evolve adaptively in response to natural selection. Many of these residues are within the β-strand/β-turn region of the PGIP LRR, including two sites known to alter inhibition specificities of bean PGIPs, but others lie outside this region. Our results complement existing molecular and biochemical studies of resistance specificity, and suggest new target amino acids for manipulating PG-inhibition. |
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