ArticleThe Journal of biological chemistry2015
Three Pseudomonas putida FNR Family Proteins with Different Sensitivities to O2.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Regulation mechanism of nitrite degradation in Lactobacillus plantarum WU14 mediated by Fnr.Archives of microbiology · 2024Article
- The Impact of Chromate onFrontiers in microbiology · 2022Article
- Transcriptome Changes inInternational journal of molecular sciences · 2020Article
- Identification of two fnr genes and characterisation of their role in the anaerobic switch in Sphingopyxis granuli strain TFA.Scientific reports · 2020Article
- Protocols for RecET-based markerless gene knockout and integration to express heterologous biosynthetic gene clusters in Pseudomonas putida.Microbial biotechnology · 2020Article
- Core regulon of the global anaerobic regulator Anr targets central metabolism functions in Pseudomonas species.Scientific reports · 2019Article
- Identification and Unusual Properties of the Master Regulator FNR in the Extreme AcidophileFrontiers in microbiology · 2019Article
- Hierarchical interactions between Fnr orthologs allows fine-tuning of transcription in response to oxygen in Herbaspirillum seropedicae.Nucleic acids research · 2018Article
- Discrimination and Integration of Stress Signals by Pathogenic Bacteria.Cell host & microbe · 2016Review
- Biochemical properties of Paracoccus denitrificans FnrP: reactions with molecular oxygen and nitric oxide.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
The Escherichia coli fumarate-nitrate reduction regulator (FNR) protein is the paradigm for bacterial O2-sensing transcription factors. However, unlike E. coli, some bacterial species possess multiple FNR proteins that presumably have evolved to fulfill distinct roles. Here, three FNR proteins (ANR, PP_3233, and PP_3287) from a single bacterial species, Pseudomonas putida KT2440, have been analyzed. Under anaerobic conditions, all three proteins had spectral properties resembling those of [4Fe-4S] proteins. The reactivity of the ANR [4Fe-4S] cluster with O2 was similar to that of E. coli FNR, and during conversion to the apo-protein, via a [2Fe-2S] intermediate, cluster sulfur was retained. Like ANR, reconstituted PP_3233 and PP_3287 were converted to [2Fe-2S] forms when exposed to O2, but their [4Fe-4S] clusters reacted more slowly. Transcription from an FNR-dependent promoter with a consensus FNR-binding site in P. putida and E. coli strains expressing only one FNR protein was consistent with the in vitro responses to O2. Taken together, the experimental results suggest that the local environments of the iron-sulfur clusters in the different P. putida FNR proteins influence their reactivity with O2, such that ANR resembles E. coli FNR and is highly responsive to low concentrations of O2, whereas PP_3233 and PP_3287 have evolved to be less sensitive to O2.
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Registered trials
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