Expression of the hemolysin operon in Escherichia coli is modulated by a nucleoid-protein complex that includes the proteins Hha and H-NS

被引：0

作者：

J. M. Nieto

C. Madrid

A. Prenafeta

E. Miquelay

C. Balsalobre

M. Carrascal

A. Juárez

机构：

[1] Departament de Microbiologia. Universitat de Barcelona,

[2] Avda. Diagonal,undefined

[3] 645,undefined

[4] 08028 Barcelona,undefined

[5] Spain Tel.: +34 93 4021487; Fax: +34 93 4110592 E-mail: juarez@porthos.bio.ub.es,undefined

[6] Espectrometría de Masas Estructural y Biológica,undefined

[7] Departamento Bioanalítica Médica,undefined

[8] IIBB,undefined

[9] IDIBARS,undefined

[10] CSIC,undefined

[11] Jordi Girona,undefined

[12] 18-26,undefined

[13] 08034 Barcelona,undefined

[14] Spain,undefined

来源：

Molecular and General Genetics MGG | 2000年 / 263卷

关键词：

Key words Hha; H-NS; Protein-protein interaction; Protein-DNA interaction; Hemolysin;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

The Escherichia coli protein Hha is a temperature- and osmolarity-dependent modulator of the expression of the hemolysin operon. The Hha protein was purified and its DNA-binding properties analyzed. Hha binds in a non-specific manner throughout the upstream regulatory region of the hemolysin operon in the recombinant hemolytic plasmid pANN202-312. A search for interacting proteins revealed that Hha interacts with H-NS. DNA-binding studies showed that, in vitro, Hha and H-NS together form a complex with DNA that differs from those formed with either protein alone. These data, together with the effects of hha and hns mutations on the expression of the hemolysin genes, suggest that in vivo H-NS and Hha form a nucleoid-protein complex that accounts for the thermo-osmotic regulation of the hemolysin operon in E. coli.

引用

页码：349 / 358

页数：9

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