Plant defensins: Common fold,multiple functions |
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| Institution: | 1. La Trobe Institute of Molecular Sciences, La Trobe University, Melbourne 3086, Australia;2. Hexima Limited, Melbourne 3000, Australia;1. Universidade Estadual do Norte Fluminense Darcy Ribeiro, Laboratório de Melhoramento Genético Vegetal, Centro de Ciências e Tecnologias Agropecuárias, Brazil;2. Universidade Estadual do Norte Fluminense Darcy Ribeiro, Laboratório de Fisiologia e Bioquímica de Microrganismos, Centro de Biociências e Biotecnologia, Brazil;3. Universidade Estadual do Norte Fluminense Darcy Ribeiro, Laboratório de Química e Função de Proteínas e Peptídeos, Centro de Biociências e Biotecnologia, Brazil;1. Laboratory of Protein Chemistry and Biochemistry, Department of Cell Biology, University of Brasilia-Federal District, Brasilia, Federal District, Brazil;2. Food Research Center – FoRC, Sao Paulo University, USP, Sao Paulo, SP, Brazil;3. Faculty of Natural Resource Sciences, School of Business and Science, University of Akureyri, Akureyri, Iceland;1. Hokkaido Agricultural Research Center, National Agriculture and Food Research Organization (NARO), Toyohira-ku, Sapporo 062-8555, Japan;2. Graduate School of Agriculture, Hokkaido University, Kita-ku, Sapporo 060-8589, Japan;3. Institute of Crop Science, National Agriculture and Food Research Organization (NARO), Kannondai, Tsukuba 305-8518, Japan;1. AAFC Lethbridge Research Centre, Lethbridge, AB, Canada;2. Sustainable Agricultural Systems Laboratory, United States Department of Agriculture, ARS''s Henry A. Wallace Beltsville Agricultural Research Center, Beltsville, MD 20705, USA |
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| Abstract: | Plant defensins represent a large class of structurally similar peptides found throughout the plant kingdom. Despite a conserved cysteine spacing pattern and three-dimensional structure, their sequences are highly divergent and they display a range of activities including antifungal and antibacterial activities, enzyme inhibitory activities as well as roles in heavy metal tolerance and development. The vast number of sequences along with their diverse range of activities makes it impossible to test the activity and assign function to all plant defensins. However, as the number of characterized defensins increases, in depth sequence analysis may allow us to predict the function of newly identified peptides. In this review, we analyze the sequences of defensins whose activities have been described and group these based on similarity using a maximum-likelihood phylogenetic tree. We also compare the amino acids that have been described as essential for the activity of various plant defensins between these groups. While many more plant defensins will need to be characterized before we can develop rules to predict the activity of novel sequences, this approach may prove useful in identifying structure–function relationships. |
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