Wheat stripe rust,due to infection by Puccinia striiformis f.sp.tritici(Pst),is a devastating disease that causes significant global grain yield losses.Yr36,which encodes Wheat Kinase START1(WKS1),is an effec-tive high-temperature adult-plant resistance gene and confers resistance to a broad spectrum of Pst races.We previously showed that WKS1 phosphorylates the thylakoid ascorbate peroxidase protein and reduces its ability to detoxify peroxides,which may contribute to the accumulation of reactive oxygen species(ROS).WKS1-mediated Pst resistance is accompanied by leaf chlorosis in Pst-infected regions,but the un-derlying mechanisms remain elusive.Here,we show that WKS1 interacts with and phosphorylates PsbO,an extrinsic member of photosystem Ⅱ(PS Ⅱ),to reduce photosynthesis,regulate leaf chlorosis,and confer Pst resistance.A point mutation in PsbO-A1 or reduction in its transcript levels by RNA interference resulted in chlorosis and reduced Pst sporulation.Biochemical analyses revealed that WKS1 phosphorylates PsbO at two conserved amino acids involved in physical interactions with PS Ⅱ and reduces the binding affinity of PsbO with PS Ⅱ.Presumably,phosphorylated PsbO proteins dissociate from the PS Ⅱ complex and then un-dergo rapid degradation by cysteine and aspartic proteases.Taken together,these results demonstrate that perturbations of wheat PsbO by point mutation or phosphorylation by WKS1 reduce the rate of photo-synthesis and delay the growth of Pst pathogen before the induction of ROS.