Abstract
Triacylglycerol lipases are class of enzymes which catalyze the hydrolysis of long-chain triglycerides. They are widely found in the plant kingdom, numerous genes putatively encoding triacylglycerol lipases are sequenced but only a few of them have been characterized. Here we systematically analyzed Arabidopsis gene sequences deposited in public databases, and identified 38 putative class III lipase proteins, all of which contain a highly conserved lipase_3 domain (Pfam ID: PF01764). These 38 genes are randomly distributed on all chromosomes, and their genomic sequences consist of variable numbers of introns from zero to 13. They can be divided into four groups based on homology of protein sequences, and their potential subcellular localization is predicted to cytosol, chloroplast, mitochondria or endoplasmic reticulum. Furthermore, ten typical genes are selected to investigate their expression patterns. Most of them show weak tissue- or organ-specificity expression pattern. Several of them significantly accumulates in some tissues or organs in addition to germinated seedlings. Some of them are specifically transcribed during seed germination while others are not detected during stages of normal growth which are probably induced by stresses. In conclusion, putative Arabidopsis class III lipases display polymorphism in their sequences, gene structures and expression patterns.
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Abbreviations
- TAG:
-
Triacylglycerol
- LID:
-
DAD1-homologous lipase
- DAD:
-
Defective in anther dehiscence protein
- AGLIP:
-
Arabidopsis putative classs III lipase
- OBL:
-
Oil body-associated lipase
- PRLIP:
-
Pathogenesis-related lipase
- NTLIP:
-
lipase_3 N-terminal domain containing lipase
- CaMBP:
-
Calmodulin-binding protein
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This work was funded by China National “863” High-Tech Program, China Ministry of Education and Shanghai Science and Technology Committee.
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Wei Li and Hua Ling are co-first authors.
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Li, W., Ling, H., Zhang, F. et al. Analysis of Arabidopsis genes encoding putative class III lipases. J. Plant Biochem. Biotechnol. 21, 261–267 (2012). https://doi.org/10.1007/s13562-011-0103-0
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DOI: https://doi.org/10.1007/s13562-011-0103-0