Ace-AMP1 In Vitro Antifungal Function And Application, As Well As Arabidopsis PARP Protein Biochemical Research

Ace-AMP1is a potent antifungal peptide found in onion (Allium cepa) seeds with sequence similarity to plant lipid transfer proteins. Transgenic plants overexpressing Ace-AMPl gene have enhanced disease resistance to some fungal pathogens. However, mass production in heterologous systems and in vitro application of this peptide have not been reported. In this study, Ace-AMP1was highly expressed in a prokaryotic Escherichia coli system as a fusion protein. The purified protein inhibited the growth of many plant fungal pathogens, especially Alternaria solani, Fusarium oxysporum f. sp. vasinfectum, and Verticillium dahliae. The inhibitory effect was accompanied by hyphal hyperbranching for V. dahliae but not for F. oxysporum f. sp.vasinfectum and A. solani, suggesting that the mode of action of Ace-AMP1on different fungi might be different. Application of Ace-AMP1on tomato leaves showed that the recombinant protein conferred strong resistance to the tomato pathogen A. solani and could be used as an effective fungicide. Poly(ADP-ribosyl)ation, catalyzed by poly(ADP-ribose) polymerases (PARPs), is an important posttranslational modification of proteins. In animals, PARPs are more extensively studied. They play important roles in DNA repairing, modulation of chromatin structure, gene transcription, cell cycle, apoptosis etc. While in plants, the function of PARPs is still not clear. Here, we confirmed the enzyme activities of PARP1and PARP2from Arabidopsis thaliana. Our results provided biochemistry evidence that PARPs are involved in the DNA repairing process in plants.