Phospholipase D （PLD, EC 3.1.4.4） plays an important role in adaptive response of postharvest fruit to environment. In this study, a novel cDNA of PLDα was isolated with the strategy of in silico cloning in combina...Phospholipase D （PLD, EC 3.1.4.4） plays an important role in adaptive response of postharvest fruit to environment. In this study, a novel cDNA of PLDα was isolated with the strategy of in silico cloning in combination with RT-PCR from peach （Prunus persica L. cv. Jiubao）. The obtained PLDα gene contained a complete open reading frame encoding a 92- kDa protein of 810 amino acid residues, which possessed the characteristic C2 domain and two catalytic HKD motifs. The alignment analysis of the deduced peach PLDa protein with other known PLDα family proteins indicated that peach PLDα was conserved and highly homologous with strawberry PLDα. Semi-quantitative RT-PCR and Northern blot analysis indicated PLDα mRNA in peach fruits could be induced by low temperature. This work provided a scientific basis for further investigating the mechanism of postharvest fruit adaptation to low temperature.展开更多
Hydrolysis reaction of L-a-dipalmitoylphosphatidylcholine (L-DPPC) monolayer with phospholipase D (PLD) has been investigated by Brewster angle microscopy (BAM) combined with the film balance. It has been found that ...Hydrolysis reaction of L-a-dipalmitoylphosphatidylcholine (L-DPPC) monolayer with phospholipase D (PLD) has been investigated by Brewster angle microscopy (BAM) combined with the film balance. It has been found that the L-DPPC domains were changed into the 搇otus?structure by PLD. It suggests that the hydrolysis reaction is incomplete and the products together with the nonreacted materials undergo a molecular rearrangement at the interface.展开更多
基金supported by China Post doctoral Science Foundation (20070420095)the National Natural Science Foundation of China (30571279,30871699,30901012)+1 种基金Innovative Foundation of Shanghai UniversitySystems Biology Research Foundation of Shanghai University
文摘Phospholipase D （PLD, EC 3.1.4.4） plays an important role in adaptive response of postharvest fruit to environment. In this study, a novel cDNA of PLDα was isolated with the strategy of in silico cloning in combination with RT-PCR from peach （Prunus persica L. cv. Jiubao）. The obtained PLDα gene contained a complete open reading frame encoding a 92- kDa protein of 810 amino acid residues, which possessed the characteristic C2 domain and two catalytic HKD motifs. The alignment analysis of the deduced peach PLDa protein with other known PLDα family proteins indicated that peach PLDα was conserved and highly homologous with strawberry PLDα. Semi-quantitative RT-PCR and Northern blot analysis indicated PLDα mRNA in peach fruits could be induced by low temperature. This work provided a scientific basis for further investigating the mechanism of postharvest fruit adaptation to low temperature.
基金supported by NNSFC(NO.29925307)as well as the research contract between the German Max-Planck-Society and the Chinese Academy of Sciences.
文摘Hydrolysis reaction of L-a-dipalmitoylphosphatidylcholine (L-DPPC) monolayer with phospholipase D (PLD) has been investigated by Brewster angle microscopy (BAM) combined with the film balance. It has been found that the L-DPPC domains were changed into the 搇otus?structure by PLD. It suggests that the hydrolysis reaction is incomplete and the products together with the nonreacted materials undergo a molecular rearrangement at the interface.
