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Diversity at the Mla Powdery Mildew Resistance Locus from Cultivated Barley Reveals Sites of Positive Selection

April 2010 , Volume 23 , Number  4
Pages  497 - 509

Sabine Seeholzer,1 Takashi Tsuchimatsu,1,2 Tina Jordan,1 Stéphane Bieri,1 Simone Pajonk,3 Wenxiang Yang,4 Ahmed Jahoor,5 Kentaro K. Shimizu,1 Beat Keller,1 and Paul Schulze-Lefert3

1Plant Biology, University of Zürich, Zürich, Switzerland; 2Department of General Systems Studies, University of Tokyo, Tokyo, Japan; 3Department of Plant--Microbe Interactions, Max-Planck-Institut für Züchtungsforschung, Köln, Germany; 4Department of Plant Pathology, Agricultural University of Hebei; Biocontrol Centre of Plant Pathogens and Pests, Hebei Province, China; 5Department of Agricultural Sciences, Copenhagen University, Frederiksberg, Denmark

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Submitted 28 October 2009.

The Mla locus in barley (Hordeum vulgare) conditions isolate-specific immunity to the powdery mildew fungus (Blumeria graminis f. sp. hordei) and encodes intracellular coiled-coil (CC) domain, nucleotide-binding (NB) site, and leucine-rich repeat (LRR)-containing receptor proteins. Over the last decades, genetic studies in breeding material have identified a large number of functional resistance genes at the Mla locus. To study the structural and functional diversity of this locus at the molecular level, we isolated 23 candidate MLA cDNAs from barley accessions that were previously shown by genetic studies to harbor different Mla resistance specificities. Resistance activity was detected for 13 candidate MLA cDNAs in a transient gene-expression assay. Sequence alignment of the deduced MLA proteins improved secondary structure predictions, revealing four additional, previously overlooked LRR. Analysis of nucleotide diversity of the candidate and validated MLA cDNAs revealed 34 sites of positive selection. Recombination or gene conversion events were frequent in the first half of the gene but positive selection was also found when this region was excluded. The positively selected sites are all, except two, located in the LRR domain and cluster in predicted solvent-exposed residues of the repeats 7 to 15 and adjacent turns on the concave side of the predicted solenoid protein structure. This domain-restricted pattern of positively selected sites, together with the length conservation of individual LRR, suggests direct binding of effectors to MLA receptors.

© 2010 The American Phytopathological Society