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Cold induction of EARLI1 , a putative Arabidopsis lipid transfer protein, is light and calcium dependent
Author(s) -
BUBIER J.,
SCHLÄPPI M.
Publication year - 2004
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.2004.01198.x
Subject(s) - egta , calcium , microbiology and biotechnology , biology , chemistry , photomorphogenesis , arabidopsis , biochemistry , biophysics , gene , mutant , organic chemistry
As sessile organisms, plants must adapt to their environment. One approach toward understanding this adaptation is to investigate environmental regulation of gene expression. Our focus is on the environmental regulation of EARLI1 , which is activated by cold and long‐day photoperiods. Cold activation of EARLI1 in short‐day photoperiods is slow, requiring several hours at 4 °C to detect an increase in mRNA abundance. EARLI1 is not efficiently cold‐activated in etiolated seedlings, suggesting that photomorphogenesis is necessary for its cold activation. Cold activation of EARLI1 is inhibited in the presence of the calcium channel blocker lanthanum chloride or the calcium chelator EGTA. Addition of the calcium ionophore Bay K8644 results in cold‐independent activation of EARLI1 . These data suggest that EARLI1 is not an immediate target of the cold response, and that calcium flux affects its expression. EARLI1 is a putative secreted protein and has motifs found in lipid transfer proteins. Over‐expression of EARLI1 in transgenic plants results in reduced electrolyte leakage during freezing damage, suggesting that EARLI1 may affect membrane or cell wall stability in response to low temperature stress.