Experimental and computer evaluation of the ability ssT-DNA-binding VirE2 protein to interact with lipid membranes

Motivation. The aim of this work was to study VirE2-protein-artificial membrane interactions and to perform a computer simulation of VirE2-protein pore-forming capacity. Results. The interaction of a VirE2-protein-ssT-DNA complex with flat black membranes was investigated. Using the "patch-clamp" method, we revealed for the first time of a single, long-time (up to 7 s) jumps of membrane conductivity (or channel formation) during coincubation with VirE2 protein in a voltage-dependent manner. It is possible that VirE2 protein forms a membrane pore for T-DNA transfer. We used porins (as beta-sheet containing) and bacteriorodopsin (as alpha-sheet containing) transmembrane proteins as models for computer comparison with VirE2 protein. Using an original program, "Graphic Imagination", we predicted from 3 to 6 beta-sheets for aquaporins and up to 15 beta-sheets for VirE2 protein and found most similarity of VirE2 protein at this trait with nucleoporins. But we did not find typical transmembrane segments for VirE2 protein by using the MEMSAT program.