Davis N G, Boeke J D, Model P
J Mol Biol. 1985 Jan 5;181(1):111-21. doi: 10.1016/0022-2836(85)90329-8.
We describe a detailed deletion analysis of the anchoring domain of a model membrane protein. Removal of the 23 contiguous uncharged amino acids from the carboxy terminus of the bacteriophage fl gene III protein (pIII) converts it from an integral membrane protein to a secreted periplasmic form. Deletions that remove six or fewer residues of the hydrophobic core result in no diminution of the protein's capacity to anchor in the membrane. Longer deletions into this hydrophobic domain gradually destablize the protein-membrane association. pIII derivatives with over half of the hydrophobic core deleted retain substantial residual anchor function. The basic residues, arginine and lysine, which provide a carboxy-terminal boundary for this domain, can be deleted without loss of anchoring capacity.
我们描述了对一种模型膜蛋白锚定结构域的详细缺失分析。从噬菌体fl基因III蛋白（pIII）的羧基末端去除23个连续的不带电荷氨基酸，可将其从整合膜蛋白转变为分泌型周质形式。去除疏水核心六个或更少残基的缺失不会降低蛋白质锚定在膜中的能力。进入该疏水结构域的更长缺失会逐渐破坏蛋白质与膜的结合。疏水核心超过一半被删除的pIII衍生物保留了相当大的残余锚定功能。为该结构域提供羧基末端边界的碱性残基精氨酸和赖氨酸可以被删除而不丧失锚定能力。
