Molecular Evolution of Lysin Motif-Type Receptor-Like Kinases in Plants

• Published in: Plant physiology (Bethesda) Vol. 144; no. 2; pp. 623 - 636
• Main Authors: Zhang, Xue-Cheng, Wu, Xiaolei, Findley, Seth, Wan, Jinrong, Libault, Marc, Nguyen, Henry T, Cannon, Steven B, Stacey, Gary
• Format: Journal Article
• Language: English
• Published: Rockville, MD American Society of Plant Biologists 01-06-2007; American Society of Plant Physiologists
• Subjects: Agronomy. Soil science and plant productions; Amino Acid Motifs - genetics; Biological and medical sciences; Classical and quantitative genetics. Population genetics. Molecular genetics; Evolution; Evolution, Molecular; Fundamental and applied biological sciences. Psychology; gene expression; Gene Expression Regulation, Plant; Generalities. Genetics. Plant material; Genes; Genetics and breeding of economic plants; Genome Analysis; Genome, Plant; Genomes; genomic microsynteny; Genomics; Glycine max; In Situ Hybridization, Fluorescence; Legumes; LYK genes; lysin motif domain; Magnoliopsida - enzymology; Magnoliopsida - genetics; messenger RNA; Molecular genetics; Molecular Sequence Data; Multigene Family; Phylogeny; plant genetics; Plant Proteins - genetics; Plants; protein kinases; Protein Kinases - genetics; Proteins; receptor kinase domain; receptor-like kinase; receptors; Rice; roots; Soybeans; Synteny; Peptidases; Molecular evolution; Enzyme; Kinase; Transferases; Hydrolases; Metalloendopeptidases; Autolysin
• ISSN: 0032-0889; 1532-2548; 1532-2548
• DOI: 10.1104/pp.107.097097

The lysin motif (LysM) domain is an ancient and ubiquitous protein module that binds peptidoglycan and structurally related molecules. A genomic survey in a large number of species spanning all kingdoms reveals that the combination of LysM and receptor kinase domains is present exclusively in plants. However, the particular biological functions and molecular evolution of this gene family remain largely unknown. We show that LysM domains in plant LysM proteins are highly diversified and that a minimum of six distinct types of LysM motifs exist in plant LysM kinase proteins and five additional types of LysM motifs exist in nonkinase plant LysM proteins. Further, motif similarities suggest that plant LysM motifs are ancient. Although phylogenetic signals are not sufficient to resolve the earliest relationships, plant LysM motifs may have arisen through common ancestry with LysM motifs in other kingdoms. Within plants, the gene family has evolved through local and segmental duplications. The family has undergone further duplication and diversification in legumes, where some LysM kinase genes function as receptors for bacterial nodulation factor. Two pairs of homeologous regions were identified in soybean (Glycine max) based on microsynteny and fluorescence in situ hybridization. Expression data show that most plant LysM kinase genes are expressed predominantly in the root and that orthologous LysM kinase genes share similar tissue expression patterns. We also examined synteny around plant LysM kinase genes to help reconstruct scenarios for the evolution of this important gene family.