Identification and phylogenetic analysis of LysM-RLK family in peanut (Fabaceae)

JOHAN STIBEN RODRIGUEZ MELO; FERNANDO IBAÑEZ; MARIA LAURA TONELLI; ADRIANA FABRA

Congreso; Fourth International Society for Computational Biology Latin America Bioinformatics Conference. (ISCB-LA); 2016

The lysin motif (LysM) is an ancient protein domain originally identified in bacterial enzymes involved in binding and degrading the cell wall component peptidoglycan (Buist et al., 2008). Typically, the motif shows ranges in length from 44 to 65 amino acid residues and a βααβ secondary structure (with some exceptions) (Mulder et al., 2006). Since identification of LysM-containing receptor-like kinases (LysM-RLKs) NFR1 and NFR5 in Lotus japonicus (Madsen et al., 2003; Radutoiu et al., 2003), this motif has attracted increasing attention in plant species. Structural analysis of LysM-RLKs shows three extracellular LysM domains (with CXC motifs in the interspacing regions), a transmembrane domain, and an intracellular protein kinase domain, reflecting a typical structure of plant kinase receptors (Zhang, et al., 2007). Molecular assays suggested that LysM-RLKs are able to trigger signal transduction pathways after perception of different ligands such as rhizobial nodulation factors (NFs) and aminosugars-containing molecules such as chitin and peptidoglycan ( Mulder et al., 2006; Smit et al., 2007). On the other hand, due to poor availability of cultivated peanut (Arachis hypogaea L.) genomic sequences, our knowledge about molecular evolution and functional characterization of LysM receptors in this plant species remains limited. Therefore, a sequence analysis of LysM-RLKs in peanut and their relation with ortologs from others legumes and non-legumes is needed in order to provide valuable information about the evolutionary process and biological functions of this important gene family.