UPTAKE ACROSS THE CELL-ENVELOPE AND INSERTION INTO THE INNER MEMBRANE OF ION CHANNEL-FORMING COLICINS IN ESCHERICHIA-COLI

被引：13

作者：

BATY, D ^{[1
]}

PATTUS, F ^{[1
]}

PARKER, M ^{[1
]}

BENEDETTI, H ^{[1
]}

FRENETTE, M ^{[1
]}

BOURDINEAUD, JP ^{[1
]}

CAVARD, D ^{[1
]}

KNIBIEHLER, M ^{[1
]}

LAZDUNSKI, C ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB,W-6900 HEIDELBERG,GERMANY

来源：

BIOCHIMIE | 1990年 / 72卷 / 2-3期

关键词：

protein translocation; protein-domains; voltage-gated channels;

D O I：

10.1016/0300-9084(90)90137-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pore-forming colicins exert their lethal effect on E coli through formation of a voltage-dependent channel in the inner (cytoplasmic-membrane) thus destroying the energy potential of sensitive cells. Their mode of action appears to involve 3 steps: i) binding to a specific receptor located in the outer membrane; ii) translocation across this membrane; iii) insertion into the inner membrane. Colicin A has been used as a prototype of pore-forming colicins. In this review, the 3 functional domains of colicin A respectively involved in receptor binding, translocation and pore formation, are defined. The components of sensitive cells implicated in colicin uptake and their interactions with the various colicin A domains are described. The 3-dimensional structure of the pore-forming domain of colicin A has been determined recently. This structure suggests a model of insertion into the cytoplasmic membrane which is supported by model membrane studies. The role of the membrane potential in channel functioning is also discussed. © 1990.

引用

页码：123 / 130

页数：8

共 63 条

[1] FUNCTIONAL DOMAINS OF COLICIN-A [J].