The Arabidopsis Chaperone J3 Regulates the Plasma Membrane H+-ATPase through Interaction with the PKS5 Kinase
文献类型： 外文期刊
作者： Yang, Yongqing 1 ; Qin, Yunxia 4 ; Xie, Changgen 1 ; Zhao, Feiyi 5 ; Zhao, Jinfeng 1 ; Liu, Dafa 4 ; Chen, Shouyi 5 ; Fug 1 ;
作者机构： 1.Natl Inst Biol Sci, Beijing 102206, Peoples R China
2.Peking Univ, Coll Life Sci, Beijing 100871, Peoples R China
3.China Agr Univ, Coll Biol Sci, State Key Lab Plant Physiol & Biochem, Beijing 100094, Peoples R China
4.Chinese Acad Trop Agr Sci, Rubber Res Inst, Minist Agr Biol Rubber Tree, Key Lab, Danzhou 571737, Hainan, Peoples R China
5.Chinese Acad Sci, Inst Genet & Dev Biol, Beijing 100101, Peoples R China
6.Univ Copenhagen, Dept Plant B
关键词： Enzymology: Biochemistry and Molecular Biophysics;Molecular Genetics: Biochemistry and Molecular Biophysics
期刊名称：PLANT CELL （ 影响因子：11.277； 五年影响因子：12.061 ）
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收录情况： SCI
摘要： The plasma membrane H+-ATPase (PM H+-ATPase) plays an important role in the regulation of ion and metabolite transport and is involved in physiological processes that include cell growth, intracellular pH, and stomatal regulation. PM H+-ATPase activity is controlled by many factors, including hormones, calcium, light, and environmental stresses like increased soil salinity. We have previously shown that the Arabidopsis thaliana Salt Overly Sensitive2-Like Protein Kinase5 (PKS5) negatively regulates the PM H+-ATPase. Here, we report that a chaperone, J3 (DnaJ homolog 3; heat shock protein 40-like), activates PM H+-ATPase activity by physically interacting with and repressing PKS5 kinase activity. Plants lacking J3 are hypersensitive to salt at high external pH and exhibit decreased PM H+-ATPase activity. J3 functions upstream of PKS5 as double mutants generated using j3-1 and several pks5 mutant alleles with altered kinase activity have levels of PM H+-ATPase activity and responses to salt at alkaline pH similar to their corresponding pks5 mutant. Taken together, our results demonstrate that regulation of PM H+-ATPase activity by J3 takes place via inactivation of the PKS5 kinase.
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