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Li + ‐regulated 1‐aminocyclopropane‐1‐carboxylate synthase gene expression in Arabidopsis thaliana
Author(s) -
Liang Xiaowu,
Shen Nancy F.,
Theologis Athanasios
Publication year - 1996
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1996.10061027.x
Subject(s) - arabidopsis , cycloheximide , arabidopsis thaliana , biology , gene expression , phosphatase , kinase , inositol , atp synthase , protein kinase a , biochemistry , phosphofructokinase 2 , gene , microbiology and biotechnology , enzyme , protein biosynthesis , receptor , mutant
Summary In Arabidopsis thaliana, 1‐aminocyclopropane‐1‐carboxylate synthase (ACS) is encoded by a multigene family consisting of at least five members whose expression is induced by hormones, developmental signals, and protein synthesis inhibition. Li + , known to interfere with the phosphoinositide (PI) second messenger system by inhibiting the activity of inositol‐phosphate phosphatases, is one of the strongest inducers of ACC synthase activity in plants. Treatment of etiolated Arabidopsis seedlings with LiCl results in a rapid induction of the ACS5 gene. Also, LiCl represses the cycloheximide (CHX)‐induced accumulation of the ACS2 mRNA. The effects of Li + on the expression of ACS5 and ACS2 are specific, dose‐dependent, and can be reversed by Ca 2+ and mimicked by the protein kinase inhibitor K‐252a. The results suggest that the regulation of some ACS genes by various inducers may involve protein kinase activity, which in turn may be controlled through an inositol 1,4,5‐triphosphate (IP 3 )‐mediated Ca 2+ mobilization. Since plants contain no Li + , the cation appears to unmask pre‐existing biochemical capacity that may be utilized by various unknown transducers during plant growth and development.