DETERMINANTS OF MEMBRANE-PROTEIN TOPOLOGY
DETERMINANTS OF MEMBRANE-PROTEIN TOPOLOGY
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DOI：
10.1073/pnas.84.23.8525
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发表时间：
1987-12-01
影响因子：
11.1
通讯作者：
BECKWITH, J
中科院分区：
文献类型：
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作者：
BOYD, D;MANOIL, C;BECKWITH, J
已使用碱性磷酸酶的融合物分析了大肠杆菌中麦芽糖转运所需的整合膜蛋白MalF的拓扑结构（EC 3.1.3.1）。这种融合菌株的性质支持MalF结构先前提出的理论依据。MalF中的几个跨膜片段可以作为输出碱性磷酸酶的信号序列。其他跨膜序列与胞质结构域结合，可以稳定地将碱性磷酸酶锚在胞质中。我们的研究结果表明，膜蛋白的胞质结构域的氨基酸序列的功能（可能是psocarboxylated氨基酸）是重要的锚定这些领域在细胞质中。这些研究结合了早期的结果表明，碱性磷酸酶融合膜蛋白可以是一个重要的辅助分析膜拓扑结构及其决定因素。
The topology of the integral membrane protein MalF, which is required for maltose transport in Escherichia coli, has been analyzed using fusions of alkaline phosphatase (EC 3.1.3.1). The properties of such fusion strains support a MalF structure previously proposed on theoretical grounds. Several transmembrane segments within MalF can act as signal sequences in exporting alkaline phosphatase. Other transmembrane sequences, in conjunction with cytoplasmic domains, can stably anchor alkaline phosphatase in the cytoplasm. Our results suggest that features of the amino acid sequence (possibly the psoitively charged amino acids) of the cytoplasmic domains of membrane proteins are important in anchoring these domains in the cytoplasm. These studies in conjunction with out earlier results show that alkaline phosphatase fusions to membrane proteins can be an important aid in analyzing membrane topology and its determinants.