ANALYSIS OF ESCHERICHIA-COLI TONB MEMBRANE TOPOLOGY BY USE OF PHOA FUSIONS

被引：79

作者：

ROOF, SK

ALLARD, JD

BERTRAND, KP

POSTLE, K

机构：

[1] WASHINGTON STATE UNIV,DEPT MICROBIOL,PULLMAN,WA 99164

[2] WASHINGTON STATE UNIV,DEPT BIOCHEM & BIOPHYS,PULLMAN,WA 99164

来源：

JOURNAL OF BACTERIOLOGY | 1991年 / 173卷 / 17期

关键词：

D O I：

10.1128/jb.173.17.5554-5557.1991

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Alkaline phosphatase (PhoA) fusions to TonB amino acids 32, 60, 125, 207, and 239 (the carboxy terminus) all showed high PhoA activity; a PhoA fusion to TonB amino acid 12 was inactive. The full-length TonB-PhoA fusion protein was associated with the cytoplasmic membrane and retained partial TonB function. These results support a model in which TonB is anchored in the cytoplasmic membrane by its hydrophobic amino terminus, with the remainder of the protein, including its hydrophobic carboxy terminus, extending into the periplasm.

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页码：5554 / 5557

页数：4

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