The signal sequence of organophosphorus hydrolase (OPH SS) from Flavobacterium sp. is composed of 29 amino acids and has a twin arginine (RR) amino acids sequence in its hydrophobic region near the N-terminal that is analogous to the twin arginine consensus motif of twin arginine translocastion (Tat) pathway. To investigate that OPH SS is dependent on which pathway between general secretion (Sec) and Tat pathways, green fluorescent protein as a Tat substrate and alkaline phosphatase as a Sec substrate were fused with OPH signal sequence, and we compared their expressions and localizations with the cases of TorA signal sequence of Tat pathway and PelB signal sequence of Sec pathway. From the results, we found interesting results because both Tat and Sec substrates were successfully translocated into the periplasmic space with comparable secretion efficiencies compared to the control sequences. We surmised that OPH SS switched its translocation pathway according to type of target protein in Escherichia coli.
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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