共 35 条
Enterobacter aerogenes OmpX, a cation-selective channel mar- and osmo-regulated
被引:48
作者:

Dupont, M
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机构: Univ Mediterranee, Fac Med, EA2197, IFR48, F-13385 Marseille 05, France

Dé, E
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h-index: 0
机构: Univ Mediterranee, Fac Med, EA2197, IFR48, F-13385 Marseille 05, France

Chollet, R
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机构: Univ Mediterranee, Fac Med, EA2197, IFR48, F-13385 Marseille 05, France

Chevalier, J
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机构: Univ Mediterranee, Fac Med, EA2197, IFR48, F-13385 Marseille 05, France

Pagès, JM
论文数: 0 引用数: 0
h-index: 0
机构: Univ Mediterranee, Fac Med, EA2197, IFR48, F-13385 Marseille 05, France
机构:
[1] Univ Mediterranee, Fac Med, EA2197, IFR48, F-13385 Marseille 05, France
[2] Univ Rouen, CNRS, UMR6522, IFRMP23, F-76821 Mont St Aignan, France
关键词:
outer membrane protein;
membrane channel;
OmpX;
regulation;
D O I:
10.1016/j.febslet.2004.05.047
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:
The ompX gene of Enterobacter aerogenes was cloned. Its overexpression induced a decrease in the major porin Omp36 production and consequently a P-lactam resistance was noted. Purified outer membrane protein X (OmpX) was reconstituted into artificial membranes and formed ion channels with a conductance of 20 pS in 1 M NaCl and a cationic selectivity. Both MarA expression and high osmolarity induced a noticeable increase of the OmpX synthesis in the E. aerogenes ATCC 13048 strain. In addition, OmpX synthesis increased under conditions in which the expression of the E. aerogenes major non-specific porins, Omp36 and Omp35, decreased. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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页码:27 / 30
页数:4
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