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Mlo, a modulator of plant defense and cell death, is a novel calmodulin-binding protein - Isolation and characterization of a rice Mlo homologue

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Schulze-Lefert,  P.
Dept. of Plant Microbe Interactions (Paul Schulze-Lefert), MPI for Plant Breeding Research, Max Planck Society;

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Cho,  M. J.
Dept. of Plant Microbe Interactions (Paul Schulze-Lefert), MPI for Plant Breeding Research, Max Planck Society;

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Zitation

Kim, M. C., Lee, S. H., Kim, J. K., Chun, H. J., Choi, M. S., Chung, W. S., et al. (2002). Mlo, a modulator of plant defense and cell death, is a novel calmodulin-binding protein - Isolation and characterization of a rice Mlo homologue. Journal of Biological Chemistry, 277(22), 19304-19314.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0012-3DD6-8
Zusammenfassung
Transient influx of Ca2+ constitutes an early event in the signaling cascades that trigger plant defense responses. However, the downstream components of defense-associated Ca2+ signaling are largely unknown. Because Ca2+ signals are mediated by Ca2+-binding proteins, including calmodulin (CaM), identification and characterization of CaM-binding proteins elicited by pathogens should provide insights into the mechanism by which Ca2+ regulates defense responses. In this study, we isolated a gene encoding rice Mlo (Oryza sativa Mlo; OsMlo) using a protein-protein interaction-based screening of a cDNA expression library constructed from pathogen-elicited rice suspension cells. OsMlo has a molecular mass of 62 kDa and shares 65% sequence identity and scaffold topology with barley Mlo, a heptahelical transmembrane protein known to function as a negative regulator of broad spectrum disease resistance and leaf cell death. By using gel overlay assays, we showed that OsMlo produced in Escherichia coli binds to soybean CaM isoform-1 (SCaM-1) in a Ca2+-dependent manner. We located a 20- amino acid CaM-binding domain (CaMBD) in the OsMlo C-terminal cytoplasmic tail that is necessary and sufficient for Ca2+- dependent CaM complex formation. Specific binding of the conserved CaMBD to CaM was corroborated by site-directed mutagenesis, a gel mobility shift assay, and a competition assay with a Ca2+/CaM-dependent enzyme. Expression of OsMlo was strongly induced by a fungal pathogen and by plant defense signaling molecules. We propose that binding of Ca2+-loaded CaM to the C-terminal tail may be a common feature of Mlo proteins.