The NapF protein of the Escherichia coli periplasmic nitrate reductase system: demonstration of a cytoplasmic location and interaction with the catalytic subunit, NapA
Abstract
The periplasmic nitrate reductase of Escherichia coli is important during anaerobic growth in low-nitrate environments. The nap operon encoding this nitrate reductase comprises seven genes including a gene,napF, that encodes a putative cytoplasmic iron–sulphur protein of uncertain subcellular location and function. In this study, N-terminal sequence analysis, cell fractionation coupled with immunoblotting and construction of LacZ and PhoA fusion proteins were used together to establish that NapF is located in the E. coli cytoplasm. A bacterial two-hybrid protein–protein interaction system was used to demonstrate that NapF interacted in the cytoplasm with the terminal oxidoreductase NapA, but that it did not self-associate or interact with other electron-transport components of the Nap system, NapC, NapG or NapH, or with another cytoplasmic component, NapD. NapF, purified as a His 6-tagged protein, exhibited spectral properties characteristic of an iron–sulphur protein. This protein was able to pull down NapA from soluble extracts of E. coli. A growth-based assay for NapF function in intact cell cultures was developed and applied to assess the effect of mutation of a number of conserved amino acids. It emerged that neither a highly conserved N-terminal double-arginine motif, nor a conserved proline motif, is essential for NapF-dependent growth. The combined data indicate that NapF plays one or more currently unidentified roles in the post-translational modification of NapA prior to the export of folded NapA via the twin-arginine translocation pathway into the periplasm.
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NapF is not considered essential for NapA maturation, although it aids in [4Fe-4S] insertion.
“NapF is not considered to be essential for NapA maturation, although it does aid in [4Fe–4S] insertion. 105,258,274”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [274]
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- Authors
- Nilavongse, A., Brondijk, T. H. C., Overton, T. W., Richardson, D. J., Leach, E. R., & Cole, J. A.
- Affiliations
- University of Birmingham (GB)
- University of East Anglia (GB)
- Venue
- Microbiology
- Publisher
- Microbiology Society
- Published
- 2006-11-01
- Volume
- 152
- Issue
- 11
- Pages
- 3227-3237
- ISSN
- 1350-0872 (ISSN-L)
- 1465-2080
- OpenAlex
- W2149866996
- Cited by
- 54
- References
- 39
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 2 · 2014: 2 · 2013: 6 · 2012: 2
- FWCI
- 4.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Microbiology (publishedVersion)
- PubMed (publishedVersion)
- University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
- UEA Digital Repository (University of East Anglia) (submittedVersion)
- Funders
- Directorate for Biological Sciences
- Biotechnology and Biological Sciences Research Council
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- Napf, napA, periplasmic nitrate reductase, Escherichia coli, protein-protein interaction, twin-arginine translocation, anaerobic nitrate reduction
- MeSH terms
- Binding Sites, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Iron-Sulfur Proteins, Operon, Protein Binding, Subcellular Fractions, Catalytic Domain, Two-Hybrid System Techniques, Escherichia coli Proteins, Periplasmic Proteins, Nitrate Reductase
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