The fusion-related hydrophobic domain of Sendai F protein can be moved through the cytoplasmic membrane of Escherichia coli.
The fusion-related hydrophobic domain of Sendai F protein can be moved through the cytoplasmic membrane of Escherichia coli.
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仙台F蛋白的融合相关疏水结构域可以穿过大肠杆菌的细胞质膜。
DOI：
10.1073/pnas.83.14.5091
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发表时间：
1986
影响因子：
11.1
通讯作者：
Hsu,MC
中科院分区：
文献类型：
--
作者：
Davis,NG;Hsu,MC
最近的工作对原核细胞膜蛋白，基因III蛋白（pIII）的大肠杆菌噬菌体f1，表明足够的疏水性的多肽片段的功能，以阻止跨细胞膜的多肽转移：串16个或更多的疏水氨基酸就足够了。仙台F蛋白的融合相关疏水结构域（FRHD）是由26个连续的不带电荷残基组成的序列，其通过疏水相互作用参与了病毒包膜和靶细胞膜的融合。由于它位于病毒膜的外部，因此该序列必须在合成过程中穿过宿主细胞膜转移。我们已经将FRHD或F蛋白膜锚（F蛋白的COOH末端区域）插入到分泌的pIII的内部位点中，所述分泌的pIII缺乏其天然膜锚。这两个疏水序列在细菌中的行为就像它们在天然真核细胞宿主中一样。F蛋白膜锚的功能是停止转移，赋予F-pIII杂合蛋白跨膜拓扑结构;然而，FRHD通过细胞质膜移动，携带该序列的衍生物分泌到周质。我们讨论了如何FRHD是兼容的通过膜，但仍然能够介导膜融合通过一个假定的疏水相互作用。
Recent work on a prokaryotic membrane protein, gene III protein (pIII) of coliphage f1, showed that polypeptide segments of sufficient hydrophobicity functioned to stop transfer of the polypeptide across the cell membrane: strings of 16 or more hydrophobic amino acids sufficed. A fusion-related hydrophobic domain (FRHD) of Sendai F protein, a sequence of 26 consecutive uncharged residues, has been implicated in the fusion of the viral membrane envelope and the target-cell membrane through a hydrophobic interaction. As it is located on the exterior of the viral membrane, this sequence must be transferred across the host-cell membrane during synthesis. We have inserted either the FRHD or the F protein membrane anchor (the COOH-terminal region of the F protein) into an internal site of a secreted pIII, which lacks its natural membrane anchor. These two hydrophobic sequences behave in the bacteria just as they do in their natural eukaryotic cell host. The F protein membrane anchor functions to stop transfer, conferring a membrane-spanning topology to the F-pIII hybrid protein; however, the FRHD is moved through the cytoplasmic membrane and derivatives carrying this sequence are secreted to the periplasm. We discuss how the FRHD is compatible with passage through the membrane and yet is still able to mediate membrane fusion through a presumed hydrophobic interaction.