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Plant Physiol, October 1999, Vol. 121, pp. 545-556
Signaling Events Leading to Crassulacean Acid Metabolism
Induction in the Common Ice Plant1
Tahar
Taybi and
John C.
Cushman*
Department of Biochemistry and Molecular Biology, 147 Noble
Research Center, Oklahoma State University, Stillwater, Oklahoma
74078
A rapid, semiquantitative reverse
transcriptase-polymerase chain reaction assay was developed to
investigate signal transduction events involved in the induction of
Crassulacean acid metabolism (CAM) in detached common ice plant
(Mesembryanthemum crystallinum) leaves. Transcript
abundance of Ppc1, a gene encoding the CAM-specific isoform of phosphoenolpyruvate carboxylase, increased
rapidly in response to osmotic stress (dehydration and mannitol), ionic stress (NaCl), and exogenous abscisic acid treatment, but failed to
accumulate in response to exogenous cytokinin or methyl jasmonate. Stress-induced accumulation of Ppc1, GapC1, and Mdh1
transcripts was inhibited by pretreating leaves with the calcium
chelator ethyleneglycol-bis(aminoethyl
ether)-N,N'-tetraacetic acid, suggesting that
extracellular calcium participates in signaling events leading to CAM
induction. Treatment of unstressed detached leaves with ionomycin, a
Ca2+ ionophore, and thapsigargin, a Ca2+-ATPase
inhibitor, enhanced Ppc1 transcript accumulation,
indicating that elevations in cytosolic [Ca2+] are likely
to participate in signaling CAM induction. Inhibitors of
Ca2+- or calmodulin-dependent protein kinases
(N-[6-aminohexyl]-5-chloro-1-napthalenesulfonamide, Lavendustin C)
and protein phosphatase 1 and 2A (okadaic acid) activity suppressed
Ppc1 transcript accumulation in response to ionic and
osmotic stresses, as well as abscisic acid treatment. These results
suggest that both protein phosphorylation and dephosphorylation events
participate in signaling during CAM induction. In contrast, pretreatment with cyclosporin A or ascomycin, inhibitors of protein phosphatase 2B activity, stimulated Ppc1 gene expression
either directly or indirectly through promoting water loss.
1
This research was supported in part by the U.S.
Department of Agriculture-National Research Initiative-Competitive
Grants Program (grant no. 95-37100-1613). Additional support was
provided by the Oklahoma Agricultural Experiment Station.
*
Corresponding author; e-mail jcushman{at}biochem.okstate.edu; fax
405-744-7799.
© 1999 American Society of Plant Physiologists
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