ArticleMolecular microbiology2018
Iron-sulfur protein maturation in Helicobacter pylori: identifying a Nfu-type cluster carrier protein and its iron-sulfur protein targets.
Article in Molecular microbiology, 2018. 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, 19 citations in OpenAlex.
- Unraveling the Role of Acetic Acid Bacteria Comparing Two Acetification Profiles From Natural Raw Materials: A Quantitative Approach inFrontiers in microbiology · 2022Article
- Structural diversity of cysteine desulfurases involved in iron-sulfur cluster biosynthesis.Biophysics and physicobiology · 2022Article
- Review
- A two-hybrid system reveals previously uncharacterized protein-protein interactions within the Helicobacter pylori NIF iron-sulfur maturation system.Scientific reports · 2021Article
- Molecular Biology and Genetic Tools to Investigate Functional Redundancy Among Fe-S Cluster Carriers in E. coli.Methods in molecular biology (Clifton, N.J.) · 2021Article
- [4Fe-4S] cluster trafficking mediated byThe Journal of biological chemistry · 2020Article
- Molecular Hydrogen Metabolism: a Widespread Trait of Pathogenic Bacteria and Protists.Microbiology and molecular biology reviews : MMBR · 2020Review
- The plastidialThe Journal of biological chemistry · 2020Article
- Site-directed mutagenesis of Campylobacter concisus respiratory genes provides insight into the pathogen's growth requirements.Scientific reports · 2018Article
- Fe-S cluster assembly in the supergroup Excavata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Helicobacter pylori is anomalous among non nitrogen-fixing bacteria in containing an incomplete NIF system for Fe-S cluster assembly comprising two essential proteins, NifS (cysteine desulfurase) and NifU (scaffold protein). Although nifU deletion strains cannot be obtained via the conventional gene replacement, a NifU-depleted strain was constructed and shown to be more sensitive to oxidative stress compared to wild-type (WT) strains. The hp1492 gene, encoding a putative Nfu-type Fe-S cluster carrier protein, was disrupted in three different H. pylori strains, indicating that it is not essential. However, Δnfu strains have growth deficiency, are more sensitive to oxidative stress and are unable to colonize mouse stomachs. Moreover, Δnfu strains have lower aconitase activity but higher hydrogenase activity than the WT. Recombinant Nfu was found to bind either one [2Fe-2S] or [4Fe-4S] cluster/dimer, based on analytical, UV-visible absorption/CD and resonance Raman studies. A bacterial two-hybrid system was used to ascertain interactions between Nfu, NifS, NifU and each of 36 putative Fe-S-containing target proteins. Nfu, NifS and NifU were found to interact with 15, 6 and 29 putative Fe-S proteins respectively. The results indicate that Nfu, NifS and NifU play a major role in the biosynthesis and/or delivery of Fe-S clusters in H. pylori.
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