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Autor(en) / Beteiligte
Titel
From defense to symbiosis: limited alterations in the kinase domain of LysM receptor-like kinases are crucial for evolution of legume-Rhizobium symbiosis
Ist Teil von
  • The Plant journal : for cell and molecular biology, 2011-01, Vol.65 (2), p.169-180
Ort / Verlag
Oxford, UK: Blackwell Publishing Ltd
Erscheinungsjahr
2011
Quelle
Wiley Online Library Journals Frontfile Complete
Beschreibungen/Notizen
  • Nitrogen-fixing symbiosis between legumes and rhizobia is initiated by the recognition of rhizobial Nod factors (NFs) by host plants. NFs are diversely modified derivatives of chitin oligosaccharide, a fungal elicitor that induces defense responses in plants. Recent evidence has shown that both NFs and chitin elicitors are recognized by structurally related LysM receptor kinases. Transcriptome analyses of Lotus japonicus roots indicated that NFs not only activate symbiosis genes but also transiently activate defense-related genes through NF receptors. Conversely, chitin oligosaccharides were able to activate symbiosis genes independently of NF receptors. Analyses using chimeric genes consisting of the LysM receptor domain of a Lotus japonicus NF receptor, NFR1, and the kinase domain of an Arabidopsis chitin receptor, CERK1, demonstrated that substitution of a portion of the αEF helix in CERK1 with the amino acid sequence YAQ from the corresponding region of NFR1 enables L. japonicus nfr1 mutants to establish symbiosis with Mesorhizobium loti. We also showed that the kinase domains of two Lotus japonicus LysM receptor kinases, Lys6 and Lys7, which also possess the YAQ sequence, suppress the symbiotic defect of nfr1. These results strongly suggest that, in addition to adaptation of extracellular LysM domains to NFs, limited alterations in the kinase domain of chitin receptors have played a crucial role in shifting the intracellular signaling to symbiosis from defense responses, thus constituting one of the key genetic events in the evolution of root nodule symbiosis in legume plants.
Sprache
Englisch
Identifikatoren
ISSN: 0960-7412
eISSN: 1365-313X
DOI: 10.1111/j.1365-313x.2010.04411.x
Titel-ID: cdi_proquest_miscellaneous_888093547
Format
Schlagworte
Adaptations, Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Arabidopsis, Arabidopsis - genetics, Arabidopsis Proteins - genetics, Arabidopsis Proteins - metabolism, Bacteria, Biological and medical sciences, Cell receptors, Cell structures and functions, CERK1, Chitin, Chitin - metabolism, defense, Evolution, Evolution, Molecular, Fundamental and applied biological sciences. Psychology, Gene expression, Gene Expression Profiling, Gene Expression Regulation, Plant - physiology, Genetic Complementation Test, Host plants, Intracellular signalling, Kinases, Legumes, Lipopolysaccharides - metabolism, Loteae - enzymology, Loteae - genetics, Loteae - microbiology, Lotus japonicus, LysM receptor kinase, Mesorhizobium - genetics, Mesorhizobium - physiology, Mesorhizobium loti, Miscellaneous, Molecular and cellular biology, molecular evolution, Molecular Sequence Data, NFR1, Nitrogen Fixation - physiology, Nod factors, oligosaccharides, Parasitism and symbiosis, Plant biology, Plant physiology and development, Plant Proteins - genetics, Plant Proteins - metabolism, Plants, Genetically Modified, Protein Kinases - chemistry, Protein Kinases - genetics, Protein Kinases - metabolism, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases - genetics, Protein-Serine-Threonine Kinases - metabolism, Receptors, Cell Surface - genetics, Receptors, Cell Surface - metabolism, Root Nodules, Plant - cytology, Root Nodules, Plant - metabolism, Root Nodules, Plant - microbiology, Roots, Sequence Alignment, Signal Transduction, Soil microorganisms, Symbiosis, Symbiosis - genetics, Symbiosis - physiology

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