Abstract

The pore-forming activity of SsoHel308 helicase from extreme thermophilic archaea Saccharolobus solfataricus has been demonstrated for the first time. This protein, embedded into rabbit erythrocyte membranes, may cause erythrocyte hemolysis. It has been shown that this enzyme forms pores in a flat artificial bilayer membrane and acts as the transformer. After embedding this enzyme into bilayer lipid membranes, the membrane conductivity alters. Taken together, our results show that SsoHel308 helicase is able to form pores in artificial bilayer membranes and, in some cases, the current that flows across the membranes shares features typical of ion channels. The short lifetime of the pores in the membrane significantly reduces the toxicity of helicase for a living cell, and the possibility of directed translocation of single-stranded DNA in the presence of ATP will enable the use of this enzyme as a molecular syringe for injecting single-stranded DNA into living cells.

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