| 초록 |
Organophosphorus hydrolase (OPH) from Flavobacterium sp. is a membrane associated homodimeric metalloenzyme and has a signal sequence in its N-terminus. We found that the signal sequence of OPH 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 (S-R-R-x-F-L-K) of twin arginine translocase (Tat) pathway. To investigate whether this sequence is dependent on Tat pathway, we used green fluorescent protein (GFP) as a cytoplasmic folding reporter. Unlike Sec pathway, Tat pathway can export correctly folded GFP into the periplasm of Escherichia coli. By using the novel Tat signal sequence of OPH, we demonstrated that foreign GFP was translocated with fully active form into the periplasmic space of E. coli. |
