Glaser-Wuttke G, Keppner J, Rasched I
Fakultät für Biologie der Universität Konstanz, F.R.G.
Biochim Biophys Acta. 1989 Nov 3;985(3):239-47. doi: 10.1016/0005-2736(89)90408-2.
The gene 3-encoded adsorption protein (g3p) of filamentous phage fd has been purified to homogeneity by using high-performance liquid chromatography. Removal of SDS from the SDS-solubilized g3p results in spontaneous oligomerization of the g3p. Reconstitution into artificial lipid bilayer membranes shows that the oligomer forms large aqueous pores that remain open for seconds and are insensitive to changes in membrane potential. The estimated diameter of the pores suggest that they are large enough to allow passage of phage single-stranded DNA. The implications of these findings for phage infection are discussed.
丝状噬菌体fd的基因3编码吸附蛋白（g3p）已通过高效液相色谱法纯化至同质状态。从十二烷基硫酸钠（SDS）增溶的g3p中去除SDS会导致g3p自发寡聚。重组到人工脂质双分子层膜中表明，该寡聚物形成大的水相孔，这些孔会保持开放数秒，并且对膜电位的变化不敏感。孔的估计直径表明它们足够大，足以允许噬菌体单链DNA通过。讨论了这些发现对噬菌体感染的影响。
