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首页> 外文期刊>Journal of Molecular Biology >PACKING OF COAT PROTEIN AMPHIPATHIC AND TRANSMEMBRANE HELICES IN FILAMENTOUS BACTERIOPHAGE M13 - ROLE OF SMALL RESIDUES IN PROTEIN OLIGOMERIZATION
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PACKING OF COAT PROTEIN AMPHIPATHIC AND TRANSMEMBRANE HELICES IN FILAMENTOUS BACTERIOPHAGE M13 - ROLE OF SMALL RESIDUES IN PROTEIN OLIGOMERIZATION

机译：纤维噬菌体M13中外壳蛋白的两亲和跨膜的包装-小残基在蛋白质寡聚中的作用

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摘要

Filamentous bacteriophage M13, an important cloning and phage display vector, is encapsulated by ca 2700 copies of its 50-residue major coat protein (gene 8). This protein occurs as a membrane protein while stably inserted into its E. coli host inner membrane, and as a coat protein upon assembly and packing onto phage DNA in the lipid-free virion. To examine the specific protein-protein interactions underlying these processes, we used a combination of randomized and saturation mutagenesis of the entire gene 8 to assess the susceptibility of each position to mutation. In the resulting library of ca 100 viable M13 mutants, ''small'' residues (Ala, Gly, Ser), which constitute the non-polar face of the N-terminal amphipathic helical segment, and a face of the hydrophobic (effective transmembrane) helical segment, were found to be highly conserved. These results support a model in which coat protein packing is stabilized by the presence within each protein subunit of two ''oligomerization segments'' i.e. specific helical regions with faces rich in small residues which function to promote the close approach of alpha-helices. (C) 1995 Academic Press Limited [References: 31]
机译：丝状噬菌体M13是一种重要的克隆和噬菌体展示载体，被其约50个残基的主要外壳蛋白（基因8）的2700份拷贝包裹。该蛋白质以膜蛋白形式存在，同时稳定地插入其大肠杆菌宿主内膜中;在组装和包装到无脂质病毒粒子的噬菌体DNA中时，以外壳蛋白形式出现。为了检查这些过程中特定的蛋白质-蛋白质相互作用，我们使用了整个基因8的随机诱变和饱和诱变相结合的方法来评估每个位置突变的敏感性。在大约100个可行的M13突变体的文库中，构成N末端两亲性螺旋段非极性面的“小”残基（Ala，Gly，Ser）和疏水性（有效跨膜）面）的螺旋段，被发现是高度保守的。这些结果支持了一种模型，其中通过两个``寡聚化片段''（即具有丰富小残基的面的特定螺旋区域）的每个蛋白质亚基中存在来稳定外壳蛋白的堆积，该小残基的功能是促进α-螺旋的紧密接近。 （C）1995 Academic Press Limited [参考号：31]

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