The genetic basis of heterosis for grain yield and its components was investigated at the single- and two-locus levels using molecular markers with an immortalized F(2) (IF(2)) population, which was developed by pair crosses among recombinant inbred lines (RILs) derived from the elite maize hybrid Yuyu22. Mid-parent heterosis of each cross in the IF(2) population was used to map heterotic quantitative trait loci. A total of 13 heterotic loci (HL) were detected. These included three HL for grain yield, seven for ear length, one for ear row number and two for 100-kernel weight. A total of 143 digenic interactions contributing to mid-parent heterosis were detected at the two-locus level involving all three types of interactions (additive x additive = AA, additive x dominance = AD or DA, dominance x dominance = DD). There were 25 digenic interactions for grain yield, 36 for ear length, 31 for ear row number and 51 for 100-kernel weight. Altogether, dominance effects of HL at the single-locus level as well as AA interactions played an important role in the genetic basis of heterosis for grain yield and its components in Yuyu22.

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SUMMARY In the absence of pathogen infection, plant effector-triggered immune (ETI) receptors are maintained in a preactivation state by intermolecular interactions with other host proteins. Pathogen effector-induced alterations activate the receptor. In Arabidopsis, the ETI receptor RPM1 is activated via bacterial effector AvrB-induced phosphorylation of the RPM1-interacting protein RIN4 at Threonine 166. We find that RIN4 also interacts with the prolyl-peptidyl isomerase (PPIase) ROC1, which is reduced upon RIN4 Thr166 phosphorylation. ROC1 suppresses RPM1 immunity in a PPIase-dependent manner. Consistent with this, RIN4 Pro149 undergoes cis/trans isomerization in the presence of ROC1. While the RIN4P149V mutation abolishes RPM1 resistance, the deletion of Pro149 leads to RPM1 activation in the absence of RIN4 phosphorylation. These results support a model in which RPM1 directly senses conformational changes in RIN4 surrounding Pro149 that is controlled by ROC1. RIN4 Thr166 phosphorylation indirectly regulates RPM1 resistance by modulating the ROC1-mediated RIN4 isomerization.