The Arabidopsis Chaperone J3 Regulates the Plasma Membrane H+-ATPase through Interaction with the PKS5 Kinase
文献类型: 外文期刊
第一作者: Yang, Yongqing
作者: Yang, Yongqing;Xie, Changgen;Zhao, Jinfeng;Guo, Yan;Yang, Yongqing;Xie, Changgen;Deng, Xing Wang;Yang, Yongqing;Guo, Yan;Qin, Yunxia;Liu, Dafa;Zhao, Feiyi;Chen, Shouyi;Fuglsang, Anja T.;Palmgren, Michael G.;Schumaker, Karen S.
作者机构:
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 )
ISSN:
年卷期:
页码:
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.
分类号: Q942
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