ArticleJournal of bacteriology2007
Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 87 citations in OpenAlex.
- An Aerobic in Vitro Cell Lysate-based Method for Fe-S Cluster Reconstitution in Recombinant Rv1460 Protein from Mycobacterium tuberculosis H37Rv.Applied biochemistry and biotechnology · 2026Article
- Use of translational fusions to express functional Klebsiella oxytoca dinitrogenase reductase in plant mitochondria.Plant molecular biology · 2026Article
- Computationally Guided Design of a Soluble, Abundant and Functional AnfH Variant for the Expression of Fe-Only Nitrogenase in Plant Mitochondria.Plant biotechnology journal · 2025Article
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- Biocontrol and Growth Promotion of Rice byJournal of microbiology and biotechnology · 2025Article
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- Mitochondria function in cytoplasmic FeS protein biogenesis.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Employing Genomic Tools to Explore the Molecular Mechanisms behind the Enhancement of Plant Growth and Stress Resilience Facilitated by aInternational journal of molecular sciences · 2024Article
- Article
- Iron Homeostasis inBiology · 2023Review
- Maturation strategy influences expression levels and cofactor occupancy in Fe-S proteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- Assembly of nitrogenase biosynthetic pathway inFrontiers in microbiology · 2023Article
- AnfO controls fidelity of nitrogenase FeFe protein maturation by preventing misincorporation of FeV-cofactor.Molecular microbiology · 2022Article
- Article
- Analysis of the Genome of the Heavy Metal Resistant and Hydrocarbon-Degrading RhizosphericInternational journal of molecular sciences · 2021Article
- Towards a Synthetic Biology Toolset for Metallocluster Enzymes in Biosynthetic Pathways: What We Know and What We Need.Molecules (Basel, Switzerland) · 2021Review
- Identification of Genes Involved in Fe-S Cluster Biosynthesis of Nitrogenase inInternational journal of molecular sciences · 2021Article
- Biosynthesis of Nitrogenase Cofactors.Chemical reviews · 2020Review
- Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20.Metallomics : integrated biometal science · 2016Review
- The DUF59 Containing Protein SufT Is Involved in the Maturation of Iron-Sulfur (FeS) Proteins during Conditions of High FeS Cofactor Demand in Staphylococcus aureus.PLoS genetics · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nitrogen-fixing organism Azotobacter vinelandii contains at least two systems that catalyze formation of [Fe-S] clusters. One of these systems is encoded by nif genes, whose products supply [Fe-S] clusters required for maturation of nitrogenase. The other system is encoded by isc genes, whose products are required for maturation of [Fe-S] proteins that participate in general metabolic processes. The two systems are similar in that they include an enzyme for the mobilization of sulfur (NifS or IscS) and an assembly scaffold (NifU or IscU) upon which [Fe-S] clusters are formed. Normal cellular levels of the Nif system, which supplies [Fe-S] clusters for the maturation of nitrogenase, cannot also supply [Fe-S] clusters for the maturation of other cellular [Fe-S] proteins. Conversely, when produced at the normal physiological levels, the Isc system cannot supply [Fe-S] clusters for the maturation of nitrogenase. In the present work we found that such target specificity for IscU can be overcome by elevated production of NifU. We also found that NifU, when expressed at normal levels, is able to partially replace the function of IscU if cells are cultured under low-oxygen-availability conditions. In contrast to the situation with IscU, we could not establish conditions in which the function of IscS could be replaced by NifS. We also found that elevated expression of the Isc components, as a result of deletion of the regulatory iscR gene, improved the capacity for nitrogen-fixing growth of strains deficient in either NifU or NifS.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.