Abstract
Salinity increases phosphoenolpyruvate carboxylase kinase (PEPCase-k) activity in sorghum leaves. This work has been focused on the mechanisms responsible for this phenomenon. The light-triggered expression of SbPPCK1 gene, accountable for the photosynthetic C4-PEPCase-k, is controlled by a complex signal transduction chain involving phospholipases C and D (PLC and PLD). These two phospholipase-derived signalling pathways were functional in salinized plants. Pharmacological agents that act on PLC (U-73122, neomycin) or PLD (n-butanol) derived signals, blocked the expression of SbPPCK1, but had little effect on PEPCase-k activity. This discrepancy was further noticed when SbPPCK1-3 gene expression and PEPCase-k activity were studied in parallel. At 172 mM, the main effect of NaCl was to decrease the rate of PEPCase-k protein turnover. Meanwhile, 258 mM NaCl significantly increased both SbPPCK1 and SbPPCK2 gene expression and/or mRNA stability. The combination of these factors contributed to maintain a high PEPCase-k activity in salinity. LiCl increased calcium-dependent protein kinase (CDPK) activity in illuminated sorghum leaves while it decreased the rate of PEPCase-k degradation. The latter effect was restrained by W7, an inhibitor of CDPK activity. Recombinant PEPCase-k protein was phosphorylated in vitro by PKA. A conserved phosphorylation motif, which can be recognized by PKA and by plant CDPKs, is present in the three PEPCase-ks proteins. Thus, it is possible that a phosphorylation event could be controlling (increasing) the stability of PEPCase-k in salinity. These results propose a new mechanism of regulation of PEPCase-k levels, and highlight the relevance of the preservation of key metabolic elements during the bulk degradation of proteins, which is commonly associated to stress.
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Abbreviations
- ABA:
-
Abscisic acid
- PI-PLC:
-
Phosphoinositide-specific phospholipase C
- PLD:
-
Phospholipase D
- CDPK:
-
Ca2+-dependent protein kinase
- IP3 :
-
Inositol-1,4,5-trisphosphate
- PEPCase:
-
Phosphoenolpyruvate carboxylase
- PEPCase-k:
-
Phosphoenolpyruvate carboxylase-kinase
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Acknowledgments
This research was supported by the Junta de Andalucía (PAI group BIO298) and BFU 2007-61431/BMC (Ministerio de Educación y Ciencia). C. Arias is in receipt of a grant from Junta de Andalucía. The authors acknowledge C. Galván-Ampudia’s generous gift of pETH16H and pGEX-KG vectors, and J Vidal, C Testerink and S Muñoz’s advice with respect to CDPK activity assay, PLD and PA measurements, and purification of recombinant proteins.
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Monreal, J.A., Arias-Baldrich, C., Pérez-Montaño, F. et al. Factors involved in the rise of phosphoenolpyruvate carboxylase-kinase activity caused by salinity in sorghum leaves. Planta 237, 1401–1413 (2013). https://doi.org/10.1007/s00425-013-1855-7
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DOI: https://doi.org/10.1007/s00425-013-1855-7