Phosphorylation of Serine Residue Modulates Cotton Di19-1 and Di19-2 Activities for Responding to Hi

• 作 者: Li-XiaQin;Xiao-YingNie;RongHu;GangLi;Wen-LiangXu;Xue-BaoLi;
• 机 构: Hubei Key Laboratory of Genetic Regulation and Integrative Biology,School of Life Sciences,Central C
• 出 处: 湖北省细胞生物学学会2015年会员代表大会暨学术研讨会
• 发表日期: 2015年期

　　Di19(drought-induced protein19)family is a novel type of Cys2/His2 zinc-fimger proteins.In this study,phosphorylation assay demonstrated that cotton Di19-1 and Di19-2(GhDi19-1/-2)proteins could be phosphorylated in vitro by the calciumdependent protein kinase(CDPK)in a Ca2+-dependent manner.Mutation of serine(Ser)site in N-terminus of GhDi 19-1 and GhDi 19-2 led to the altered subcellular localization of the two proteins in cells.GhDi19-1 and GhDi19-2 overexpression transgenic Arabidopsis seedlings displayed the hypersensitivity to high salinity and abscisic acid(ABA).