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Calmodulin interacts with MLO protein to regulate defence against mildew in barley
Kim, Min-C.,Ralph Panstruga,Candance Elliott,Judith Muller,Alessandra Devoto,Yoon, Hae W.,Park, Hyeong C.,Cho, Moo J.,Paul Schulze-Lefert Plant molecular biology and biotechnology research 2002 Plant molecular biology and biotechnology research Vol.2002 No.-
In plants, defence against specific isolates of a pathogen can be triggered by the presence of a corresponding race-specific resistance gene, whereas resistance of a more broad-spectrum nature can result from recessive, presumably loss-of-regulatory-function, mutations. An example of the latter are mlo mutations in barley, which have been successful in agriculture for the control of powdery mildew fungus (Blumeria graminist f. sp. hordei; Bgh). MLO protein resides in the plasma membrane, has seven transmembrane domains, and is the prototype of a sequence-diversified family unique to plants, reminiscent of the seven-transmembrane receptors in fungi and animals. In animals, these are known as G-protein-coupled receptors and exist in three main families, lacking sequence similarity, that are thought to be an example of molecular convergence. MLO seems to function independently of heterotrimeric G proteins. We have identified a domain in MLO that mediates a Ca^(2+)-dependent interaction with calmodulin in vitro. Loss of calmodulin binding halves the ability of MLO to negatively regulate defence against powdery mildew in vivo. We propose a sensor sole for MLO in the modulation of defence reactions.