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首页> 外文期刊>Journal of bacteriology >Membrane topology of Escherichia coli diacylglycerol kinase.
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Membrane topology of Escherichia coli diacylglycerol kinase.

机译：大肠杆菌二酰基甘油激酶的膜拓扑。

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摘要

The topology of Escherichia coli diacylglycerol kinase (DAGK) within the cytoplasmic membrane was elucidated by a combined approach involving both multiple aligned sequence analysis and fusion protein experiments. Hydropathy plots of the five prokaryotic DAGK sequences available were uniform in their prediction of three transmembrane segments. The hydropathy predictions were experimentally tested genetically by fusing C-terminal deletion derivatives of DAGK to beta-lactamase and beta-galactosidase. Following expression, the enzymatic activities of the chimeric proteins were measured and used to determine the cellular location of the fusion junction. These studies confirmed the hydropathy predictions for DAGK with respect to the number and approximate sequence locations of the transmembrane segments. Further analysis of the aligned DAGK sequences detected probable alpha-helical N-terminal capping motifs and two amphipathic alpha-helices within the enzyme. The combined fusion and sequence data indicate that DAGK is a polytopic integral membrane protein with three transmembrane segments with the N terminus of the protein in the cytoplasm, the C terminus in the periplasmic space, and two amphipathic helices near the cytoplasmic surface.
机译：通过涉及多个比对序列分析和融合蛋白实验的组合方法阐明了细胞质膜内的大肠杆菌二酰基甘油激酶（DAGK）的拓扑。可用的五个原核DAGK​​序列的亲水性图在其三个跨膜片段的预测中是一致的。通过将DAGK的C端缺失衍生物与β-内酰胺酶和β-半乳糖苷酶融合，对遗传反应进行了遗传测试。表达后，测量嵌合蛋白的酶活性，并用于确定融合接头的细胞位置。这些研究证实了DAGK关于跨膜区段的数目和近似序列位置的亲水性预测。对比对的DAGK序列的进一步分析检测到了酶中可能的α-螺旋N末端加帽基序和两个两亲性α-螺旋。融合的融合和序列数据表明，DAGK是具有三个跨膜片段的多位整合膜蛋白，其蛋白的N端位于细胞质中，C端位于周质空间中，两个两亲螺旋位于细胞质表面附近。

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