Sphingosine-1-phosphate lyase （SPL） is involved in degrading the conserved sphingolipid signaling molecule sphingosine-1-phosphate. However, molecular studies on plant SPL have not been reported to date. Here, we pr...Sphingosine-1-phosphate lyase （SPL） is involved in degrading the conserved sphingolipid signaling molecule sphingosine-1-phosphate. However, molecular studies on plant SPL have not been reported to date. Here, we present bioinformatic, molecular and functional analyses of putative SPL proteins from Arabidopsis thaliana and rice （designated as AtSPL and OsSPL, respectively）. Amino acid sequence comparison revealed that plant SPL contalned the pyridoxal-dependent decarboxylase domain and the conserved residue that may be involved in substrate catalysis. When expressed in Saccharomyces cerevisiae, AtSPL and OsSPL corrected the hypersensitive phenotype of the yeast dpl1 deletion strain, which is deficient in endogenous SPL activity, to exogenous supplied sphingolipid long chain bases （LCBs）, suggesting that plant SPL protein is functional In vivo in degrading phosphorylated LCBs. In Arabidopsis, AtSPL transcripts were detected in roots, stems, leaves, flowers and siliques. In pAtSPL-AtSPL∷GUS transgenic lines, the AtSPL∷GUS fusion protein was found in a variety of vegetative and reproductive tissues. AtSPL expression level was dynamically regulated during leaf development and senescence, and was steadily and significantly increased in Arabidopsis seedlings treated with the cell death-inducing fungal toxin fumonisin B1. The potential function of SPL in Arabidopsis is discussed.展开更多
基金Supported by the National Natural Science Foundation of China （30521001） and the Chinese Academy of Sciences （KSCX2-SW-304）.Acknowledgments The authors are grateful to Drs Lu Liang and Yiping Tong for helpful discussion on this work and the writing of the manuscript.
文摘Sphingosine-1-phosphate lyase （SPL） is involved in degrading the conserved sphingolipid signaling molecule sphingosine-1-phosphate. However, molecular studies on plant SPL have not been reported to date. Here, we present bioinformatic, molecular and functional analyses of putative SPL proteins from Arabidopsis thaliana and rice （designated as AtSPL and OsSPL, respectively）. Amino acid sequence comparison revealed that plant SPL contalned the pyridoxal-dependent decarboxylase domain and the conserved residue that may be involved in substrate catalysis. When expressed in Saccharomyces cerevisiae, AtSPL and OsSPL corrected the hypersensitive phenotype of the yeast dpl1 deletion strain, which is deficient in endogenous SPL activity, to exogenous supplied sphingolipid long chain bases （LCBs）, suggesting that plant SPL protein is functional In vivo in degrading phosphorylated LCBs. In Arabidopsis, AtSPL transcripts were detected in roots, stems, leaves, flowers and siliques. In pAtSPL-AtSPL∷GUS transgenic lines, the AtSPL∷GUS fusion protein was found in a variety of vegetative and reproductive tissues. AtSPL expression level was dynamically regulated during leaf development and senescence, and was steadily and significantly increased in Arabidopsis seedlings treated with the cell death-inducing fungal toxin fumonisin B1. The potential function of SPL in Arabidopsis is discussed.
