Calmodulin interacts with MLO protein to regulate defence against mildew in barley

Min C. Kim, Ralph Panstruga, Candace Elliott, Judith Müller, Alessandra Devoto, Hae W. Yoon, Hyeong C. Park, Moo J. Cho () and Paul Schulze-Lefert ()
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Min C. Kim: Gyeongsang National University
Ralph Panstruga: Max-Planck-Institut für Züchtungsforschung
Candace Elliott: The Sainsbury Laboratory, John Innes Centre
Judith Müller: Max-Planck-Institut für Züchtungsforschung
Alessandra Devoto: The Sainsbury Laboratory, John Innes Centre
Hae W. Yoon: Gyeongsang National University
Hyeong C. Park: Gyeongsang National University
Moo J. Cho: Gyeongsang National University
Paul Schulze-Lefert: Max-Planck-Institut für Züchtungsforschung

Nature, 2002, vol. 416, issue 6879, 447-451

Abstract: Abstract In plants, defence against specific isolates of a pathogen can be triggered by the presence of a corresponding race-specific resistance gene1, whereas resistance of a more broad-spectrum nature can result from recessive, presumably loss-of-regulatory-function, mutations2. An example of the latter are mlo mutations in barley, which have been successful in agriculture for the control of powdery mildew fungus (Blumeria graminis f. sp. hordei; Bgh)3. MLO protein resides in the plasma membrane, has seven transmembrane domains, and is the prototype of a sequence-diversified family unique to plants4,5, reminiscent of the seven-transmembrane receptors in fungi and animals5. 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 convergence6. MLO seems to function independently of heterotrimeric G proteins. We have identified a domain in MLO that mediates a Ca2+-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 role for MLO in the modulation of defence reactions.

Date: 2002
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DOI: 10.1038/416447a

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