首页 | 官方网站   微博 | 高级检索  
     


Light as a signal influencing the phosphorylation status of plant proteins
Authors:Budde R J  Randall D D
Affiliation:Department of Biochemistry, 117 Schweitzer Hall, University of Missouri, Columbia, Missouri 65211.
Abstract:The phosphorylation-status of a number of plant enzymes has been shown to be altered in response to light. Phosphoenolpyruvate carboxylase is phosphorylated (more active) in C4 plants in the light but CAM phosphoenolpyruvate carboxylase is phosphorylated (more active) in the dark. C4 plant pyruvate, Pi dikinase is dephosphorylated (activated) in the light and sucrose phosphate synthase is less phosphorylated (more active) in the light. The mitochondrial pyruvate dehydrogenase is inactivated (phosphorylated) in the light. The reversal of these events occurs in the dark or when photosynthesis is inhibited. Phytochrome and blue light receptors also alter the phosphorylation-status of proteins. The evidence is rapidly increasing in support of signal transduction networks in plants that involve light reception.
Keywords:
本文献已被 PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司    京ICP备09084417号-23

京公网安备 11010802026262号