Authors: Ionit Iberkleid Adva Yeheskel Eduard Belausov B Chinnapandi N Fitoussi Sigal Brown Miyara
Publish Date: 2015/05/17
Volume: 143, Issue: 1, Pages: 133-149
Abstract
Plantparasitic nematodes are extremely destructive pathogens with a cosmopolitan distribution and a host range that affects most crops They are characterized by distinct parasitic lifestyles eg as sedentary or migratory endo or ectoparasites resulting in high losses in yield and revenue Possessing limited lipid metabolism they produce one or two structurally unique classes of small αhelixrich fatty acid and retinol binding FAR proteins that have no counterpart in other organisms We investigated the sequence and structural characteristics of the FAR protein of the rootknot nematode Meloidogyne javanica MjFAR1 in comparison to other studied FAR proteins Protein sequence analyses enabled phylogenetic clustering according to trophic groups and lifestyles Bioinformatics analysis of the FAR protein sequences revealed ten likely core amino acids representing the trophicgroup clustering Clear modifications of four of these amino acids from less reactive nonpolar with aliphatic R group to more reactive positively or negatively charged R groups or uncharged polar R groups might distinguish freeliving from parasitic nematode species Structural predictions of the mature MjFAR1 protein and its ligandbinding pockets suggest that adaptation toward parasitism is associated with increased reactivity of the second pocket residues as well as those on the protein surface Subcellular localization of MjFAR1 with or without its signal peptide was determined by Agrobacterium infiltration of Nterminal mCherrytagged protein into Nicotiana benthamiana leaves Intact MjFAR1 with its signal peptide was predominantly localized along the plasma membrane surrounding plant cells while removing the signal peptide resulted in additional localization within the cell nucleus The nuclear localization agreed with insilico analysis of the MjFAR1 sequence and sheds new light on its function in manipulating the plant response Our study provides the first basic structural information and subcellular localization of the plantparasitic MjFAR1 protein
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