Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1991 Sep;173(18):5800-7.
doi: 10.1128/jb.173.18.5800-5807.1991.

Integration host factor binds specifically to multiple sites in the ompB promoter of Escherichia coli and inhibits transcription

Affiliations

Integration host factor binds specifically to multiple sites in the ompB promoter of Escherichia coli and inhibits transcription

P Tsui et al. J Bacteriol. 1991 Sep.

Abstract

Escherichia coli integration host factor (IHF) is a DNA-binding protein that participates in gene regulation, site-specific recombination, and other processes in E. coli and some of its bacteriophages and plasmids. In the present study, we showed that IHF is a direct negative effector of the ompB operon of E. coli. Gel retardation experiments and DNase I footprinting studies revealed that IHF binds to three sites in the ompB promoter region. In vitro transcription from ompB promoter fragments was specifically blocked by IHF. In vivo experiments showed that IHF is a negative effector of ompB expression in growing cells. Analysis of IHF binding site mutations strongly suggested that IHF binding in the ompB promoter region is necessary for the negative effects seen in vivo.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Proc Natl Acad Sci U S A. 1989 Oct;86(19):7346-50 - PubMed
    1. FEBS Lett. 1990 Feb 12;261(1):19-22 - PubMed
    1. Nucleic Acids Res. 1988 Apr 25;16(8):3313-26 - PubMed
    1. Microbiol Rev. 1987 Sep;51(3):301-19 - PubMed
    1. Cell. 1987 Dec 4;51(5):699-707 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources