Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase.
Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase.
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双精氨酸蛋白转位酶 TatB 成分的膜外域特征。
DOI：
10.1016/j.febslet.2011.01.016
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发表时间：
2011
期刊：
影响因子：
3.5
通讯作者：
Maldonado B
中科院分区：
文献类型：
--
作者：
Maldonado B
双精氨酸蛋白转运（达特）系统将折叠的蛋白质转运穿过细菌的细胞质膜和植物的类囊体膜，并且在大肠杆菌中，它包括TatA、TatB和TatC组分。在这项研究中，我们表明，TatB的膜外结构域与至少一个其他TatB蛋白形成平行接触。截短TatB的C-末端三分之二仍然允许与TatC形成复合物，尽管蛋白质转运严重受损。我们无法分离出tatB中的转运失活单密码子取代突变，这表明TatB的精确氨基酸序列对其功能并不重要。结构性摘要：TatA通过双杂交与TatA物理相互作用（View相互作用）TatB和TatC通过分子筛结合（View相互作用）TatB通过双杂交与TatB物理相互作用（View相互作用1，2）
The twin arginine protein transport (Tat) system transports folded proteins across cytoplasmic membranes of bacteria and thylakoid membranes of plants, and in Escherichia coli it comprises TatA, TatB and TatC components. In this study we show that the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein. Truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised. We were unable to isolate transport-inactive single codon substitution mutations in tatB suggesting that the precise amino acid sequence of TatB is not critical to its function. STRUCTURED SUMMARY: TatAphysically interacts with TatA by two hybrid(View interaction) TatB and TatCbind by molecular sieving(View interaction) TatBphysically interacts with TatB by two hybrid (View Interaction 1, 2)