Calcium(Ca^(2+))/calmodulin(CaM)-dependent protein kinase(CCaMK)is an important positive regulator of antioxidant defenses and tolerance against oxidative stress.However,the underlying molecular mechanisms are largely...Calcium(Ca^(2+))/calmodulin(CaM)-dependent protein kinase(CCaMK)is an important positive regulator of antioxidant defenses and tolerance against oxidative stress.However,the underlying molecular mechanisms are largely unknown.Here,we report that the rice(Oryza sativa)CCa MK(OsDMI3)physically interacts with and phosphorylates OsUXS3,a cytosol-localized UDP-xylose synthase.Genetic and biochemical evidence demonstrated that OsUXS3 acts downstream of OsDMI3 to enhance the oxidative stress tolerance conferred by higher catalase(CAT)activity.Indeed,OsUXS3 interacted with CAT isozyme B(OsCATB),and this interaction was required to increase OsCATB protein abundance under oxidative stress conditions.Furthermore,we showed that OsDMI3 phosphorylates OsUXS3 on residue Ser-245,thereby further promoting the interaction between OsUXS3 and OsCATB.Our results indicate that OsDMI3 promotes the association of OsUXS3 with OsCATB to enhance CAT activity under oxidative stress.These findings reveal OsUXS3 as a direct target of OsDMI3 and demonstrate its involvement in antioxidant defense.展开更多
基金supported by the National Natural Science Foundation of China(Grant Nos 31671606,31971824,and 32170316)the Fundamental Research Funds for the Central Universities。
文摘Calcium(Ca^(2+))/calmodulin(CaM)-dependent protein kinase(CCaMK)is an important positive regulator of antioxidant defenses and tolerance against oxidative stress.However,the underlying molecular mechanisms are largely unknown.Here,we report that the rice(Oryza sativa)CCa MK(OsDMI3)physically interacts with and phosphorylates OsUXS3,a cytosol-localized UDP-xylose synthase.Genetic and biochemical evidence demonstrated that OsUXS3 acts downstream of OsDMI3 to enhance the oxidative stress tolerance conferred by higher catalase(CAT)activity.Indeed,OsUXS3 interacted with CAT isozyme B(OsCATB),and this interaction was required to increase OsCATB protein abundance under oxidative stress conditions.Furthermore,we showed that OsDMI3 phosphorylates OsUXS3 on residue Ser-245,thereby further promoting the interaction between OsUXS3 and OsCATB.Our results indicate that OsDMI3 promotes the association of OsUXS3 with OsCATB to enhance CAT activity under oxidative stress.These findings reveal OsUXS3 as a direct target of OsDMI3 and demonstrate its involvement in antioxidant defense.
