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Molecular and Functional Characterization of Sphingosine‐1‐Phosphate Lyase Homolog from Higher Plants
Author(s) -
Niu Yan,
Chen Kunling,
Wang Jizhou,
Liu Xin,
Qin Huanju,
Zhang Aimin,
Wang Daowen
Publication year - 2007
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/j.1744-7909.2007.00446.x
Subject(s) - arabidopsis , biology , arabidopsis thaliana , biochemistry , silique , saccharomyces cerevisiae , lyase , sphingolipid , microbiology and biotechnology , yeast , enzyme , gene , mutant
Sphingosine‐1‐phosphate lyase (SPL) is involved in degrading the conserved sphingolipid signaling molecule sph‐ingosine‐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 contained 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.