MEMBRANE TOPOLOGY MODEL OF ESCHERICHIA-COLI ALPHA-KETOGLUTARATE PERMEASE BY PHOA FUSION ANALYSIS

被引：30

作者：

SEOL, WG ^{[1
]}

SHATKIN, AJ ^{[1
]}

机构：

[1] CTR ADV BIOTECHNOL & MED,679 HOES LANE,PISCATAWAY,NJ 08854

来源：

JOURNAL OF BACTERIOLOGY | 1993年 / 175卷 / 02期

关键词：

D O I：

10.1128/JB.175.2.565-567.1993

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：565 / 567

页数：3

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