In vivo requirement of integration host factor for nar (nitrate reductase) operon expression in Escherichia coli K-12
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The nitrate reductase operon (narGHJI) of Escherichia coli encodes an anaerobic respiratory enzyme. Previous work has identified two cis-acting sites in the nar operon control region: a proximal site required for anaerobic induction mediated by the activator Fnr and a remote upstream site required for nitrate induction mediated by the activator NarL [Li, S. & DeMoss, J. A. (1988) J. Biol. Chem. 263, 13700-13705]. Our search for nar regulatory mutants yielded one strain with a mutation in himD, the structural gene for one of the subunits of integration host factor (IHF). Strains carrying null alleles of the IHF structural genes, himD and himA, had severe defects in nitrate induction of the nar operon but were normal for nitrate induction of the coordinately regulated fdn operon. Anaerobic expression of both operons was normal in him mutants. Gel-mobility-shift and DNase I protection experiments revealed a single IHF binding site in the nar operon control region, located midway between the upstream activation site and the promoter. We conclude that an IHF-mediated DNA bend is essential for efficient nitrate induction of the sigma 70-dependent nar operon promoter. This requirement of IHF for transcriptional activation had been noted for several sigma 54-dependent promoters.
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NarGHI is highly oxygen-responsive, under primary transcriptional control via the oxygen sensor FNR, and appears to be the major contributor to respiratory anaerobic activity.
“The first, NarGHI, is highly oxygen-responsive, under primary transcriptional control via the oxygen sensor fumarate nitrate reductase regulator (FNR), and appears to be the major contributor to respiratory anaerobic activity[256–258].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [257]
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- Authors
- Rabin, R. S., Collins, L. A., & Stewart, V
- Affiliations
- Cornell University (US)
- ORCID
- Stewart, V
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1992-09-15
- Volume
- 89
- Issue
- 18
- Pages
- 8701-8705
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC49988
- OpenAlex
- W2079660114
- Cited by
- 44
- References
- 43
- Citations by year
- 2019: 1 · 2016: 1 · 2015: 1 · 2014: 4
- FWCI
- 3.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (T32GM-07616, T32GM007616, R01 GM36877, R01GM036877)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Keywords
- integration host factor, Escherichia coli K-12, HIMA, nitrate induction, transcriptional regulation, DNA bending, FNR, NarL, anaerobic induction
- MeSH terms
- Bacterial Proteins, Base Sequence, DNA-Binding Proteins, Escherichia coli, Genes, Bacterial, Molecular Sequence Data, Nitrate Reductases, Operator Regions, Genetic, Operon, Regulatory Sequences, Nucleic Acid, Transcription, Genetic, Gene Expression Regulation, Bacterial, Integration Host Factors, Nitrate Reductase
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