tailieunhanh - Báo cáo khoa học: Lipins from plants are phosphatidate phosphatases that restore lipid synthesis in apah1Dmutant strain of Saccharomyces cerevisiae

The identification of the yeastphosphatidate phosphohydrolase(PAH1) gene encoding an enzyme with phosphatidate phosphatase (PAP; 3-sn-phosphati-date phosphohydrolase, EC ) activity led to the discovery of mam-malianLipinsand subsequently to homologous genes from plants. In the present study, we describe the functional characterization ofArabidopsis and Brassica napushomologs ofPAH1. | IFEBS Journal Lipins from plants are phosphatidate phosphatases that restore lipid synthesis in a pahlD mutant strain of Saccharomyces cerevisiae Elzbieta Mietkiewska1 Rodrigo M. P. Siloto1 Jay Dewald2 Saleh Shah3 David N. Brindley2 and Randall J. Weselake1 1 Department of Agricultural Food and NutritionalScience University of Alberta Edmonton Canada 2 Department of Biochemistry SignalTransduction Research Group Schoolof Molecular and Systems Medicine University of Alberta Edmonton Canada 3 Plant Biotechnology Alberta Innovates-Technology Futures Vegreville Canada Keywords lipin phosphatidate phosphatase Saccharomyces cerevisiae subcellular localization triacylglycerol Correspondence R. J. Weselake AgriculturalLipid Biotechnology Program Department of Agricultural Food and Nutritional Science 4-10 Agriculture Forestry Centre University of Alberta Edmonton Alberta T6G 2P5 Canada Fax 1 780 492 6739 Tel 1 780 492 4401 E-mail Received 21 September 2010 revised 10 December 2010 accepted 20 December 2010 doi The identification of the yeast phosphatidate phosphohydrolase PAH1 gene encoding an enzyme with phosphatidate phosphatase PAP 3-sn-phosphati-date phosphohydrolase EC activity led to the discovery of mammalian Lipins and subsequently to homologous genes from plants. In the present study we describe the functional characterization of Arabidopsis and Brassica napus homologs of PAH1. Recombinant expression studies confirmed that homologous PAHs from plants can rescue different phenotypes exhibited by the yeast pah1D strain such as temperature growth sensitivity and atypical neutral lipid composition. Using this expression system we examined the role of the putative catalytic motif DXDXT and other conserved residues by mutational analysis. Mutants within the carboxy-terminal lipin domain displayed significantly decreased PAP activity which was reflected by their limited ability to complement different

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