Membrane topology model of Escherichia coli alpha-ketoglutarate permease by phoA fusion analysis
Membrane topology model of Escherichia coli alpha-ketoglutarate permease by phoA fusion analysis
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DOI：
10.1128/jb.175.2.565-567.1993
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发表时间：
1993-01
影响因子：
3.2
通讯作者：
W. Seol;A. Shatkin
中科院分区：
文献类型：
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作者：
W. Seol;A. Shatkin
大肠杆菌α -酮戊二酸透酶（KgtP）是一种由432个氨基酸组成的蛋白质，与α -酮戊二酸和质子结合。根据计算的亲水剖面，预测KgtP包含12个跨膜结构域。通过KgtP - phoa基因融合和测定表达该嵌合蛋白的细胞的碱性磷酸酶活性，分析了KgtP的膜拓扑模型。磷酸酶活性水平和KgtP- phoa连接位置的比较与预测的KgtP膜拓扑模型一致。
Escherichia coli alpha-ketoglutarate permease (KgtP) is a 432-amino-acid protein that symports alpha-ketoglutarate and protons. KgtP was predicted to contain 12 membrane-spanning domains on the basis of a calculated hydropathy profile. The membrane topology model of KgtP was analyzed by using kgtP-phoA gene fusions and measuring alkaline phosphatase activities in cells expressing the chimeric proteins. Comparisons of the phosphatase activity levels and the locations of the KgtP-PhoA junctions are consistent with the predicted membrane topology model of KgtP.