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Background  Recessively inherited natural and induced mutations in the barley  Mlo  gene confer durable broad-spectrum resistance against the powdery mildew pathogen,  Blumeria graminis  f.sp.  hordei .  Mlo  codes for a member of a plant-specific family of polytopic integral membrane proteins with unknown biochemical activity. Resistant barley  mlo  mutant alleles identify amino acid residues that are critical for Mlo function in the context of powdery mildew susceptibility.    Results  We molecularly analyzed a novel set of induced barley  mlo  mutants and used site-directed mutagenesis in combination with transient gene expression to unravel novel amino acid residues of functional significance. We integrate these results with previous findings to map functionally important regions of the heptahelical Mlo protein. Our data reveal the second and third cytoplasmic loop as being particularly sensitive to functional impediment by mutational perturbation, suggesting that these regions are critical for the susceptibility-conferring activity of the Mlo protein. In contrast, only mutations in the second but not the third cytoplasmic loop appear to trigger the Endoplasmic Reticulum-localized quality control machinery that ensures the biogenesis of properly folded membrane proteins.    Conclusion  Our findings identify functionally important regions of the polytopic barley Mlo protein and reveal the differential sensitivity of individual protein domains to cellular quality control.

bmc plant biology

Novel induced mlo mutant alleles in combination with site-directed mutagenesis reveal functionally important domains in the heptahelical barley Mlo protein