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：99

作者：

Nieto, JM

Madrid, C

Prenafeta, A

Miquelay, E

Balsalobre, C

Carrascal, M

Juárez, A

机构：

[1] Univ Barcelona, Dept Microbiol, E-08028 Barcelona, Spain

[2] CSIC, IDIBARS, IIBB, Dept Bioanalit Med, Barcelona, Spain

来源：

MOLECULAR AND GENERAL GENETICS | 2000年 / 263卷 / 02期

关键词：

Hha; H-NS; protein-protein interaction; protein-DNA interaction; hemolysin;

D O I：

10.1007/s004380051178

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 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.

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收藏

页码：349 / 358

页数：10

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