ArticleJournal of bacteriology2010
SufU is an essential iron-sulfur cluster scaffold protein in Bacillus subtilis.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Structural heterogeneity of iron-sulfur cluster scaffold protein IscU: Metamorphic or partially folded?Structural dynamics (Melville, N.Y.) · 2026Review
- Intricacies in iron-sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme specificity.RSC chemical biology · 2026Review
- Structural and mechanistic insights into the sulfur transfer protein SufU from Staphylococcus aureus.Journal of inorganic biochemistry · 2026Article
- A Key Metabolic Protein in Active Mycobacterium tuberculosis: Insights into Carbon, Nitrogen, and Sulfur Metabolism.Advances in experimental medicine and biology · 2026Review
- A minimal SufBMicrobiology spectrum · 2025Article
- Methanotroph Methylotuvimicrobium alcaliphilum 20Z-3E as a fumarate producer: transcriptomic analysis and the role of malic enzyme.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- The minimal SUF system is not required for Fe-S cluster biogenesis in the methanogenic archaeon Methanosarcina acetivorans.Scientific reports · 2023Article
- The circadian clock of the bacteriumScience advances · 2023Article
- Structural and Biochemical Characterization ofBiomolecules · 2023Article
- Structural and Biochemical Characterization ofACS omega · 2022Article
- Tailored Pyridoxal Probes Unravel Novel Cofactor-Dependent Targets and Antibiotic Hits in Critical Bacterial Pathogens.Angewandte Chemie (International ed. in English) · 2022Article
- SufB intein splicing in Mycobacterium tuberculosis is influenced by two remote conserved N-extein histidines.Bioscience reports · 2022Article
- Structural diversity of cysteine desulfurases involved in iron-sulfur cluster biosynthesis.Biophysics and physicobiology · 2022Article
- The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis.Antioxidants (Basel, Switzerland) · 2021Review
- The sulfur formation system mediating extracellular cysteine-cystine recycling in Fervidobacterium islandicum AW-1 is associated with keratin degradation.Microbial biotechnology · 2021Article
- Identification of Genes Involved in Fe-S Cluster Biosynthesis of Nitrogenase inInternational journal of molecular sciences · 2021Article
- Characterization of Fe-S Clusters in Proteins by Mӧssbauer Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Fe-S cluster biogenesis by the bacterial Suf pathway.Biochimica et biophysica acta. Molecular cell research · 2020Review
- SufR, a [4Fe-4S] Cluster-Containing Transcription Factor, Represses theApplied and environmental microbiology · 2020Article
- Single-step Replacement of an Unreactive C-H Bond by a C-S Bond Using Polysulfide as the Direct Sulfur Source in Anaerobic Ergothioneine Biosynthesis.ACS catalysis · 2020Article
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Authors and funding
8 authors.
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Abstract
Bacteria use three distinct systems for iron-sulfur (Fe/S) cluster biogenesis: the ISC, SUF, and NIF machineries. The ISC and SUF systems are widely distributed, and many bacteria possess both of them. In Escherichia coli, ISC is the major and constitutive system, whereas SUF is induced under iron starvation and/or oxidative stress. Genomic analysis of the Fe/S cluster biosynthesis genes in Bacillus subtilis suggests that this bacterium's genome encodes only a SUF system consisting of a sufCDSUB gene cluster and a distant sufA gene. Mutant analysis of the putative Fe/S scaffold genes sufU and sufA revealed that sufU is essential for growth under minimal standard conditions, but not sufA. The drastic growth retardation of a conditional mutant depleted of SufU was coupled with a severe reduction of aconitase and succinate dehydrogenase activities in total-cell lysates, suggesting a crucial function of SufU in Fe/S protein biogenesis. Recombinant SufU was devoid of Fe/S clusters after aerobic purification. Upon in vitro reconstitution, SufU bound an Fe/S cluster with up to approximately 1.5 Fe and S per monomer. The assembled Fe/S cluster could be transferred from SufU to the apo form of isopropylmalate isomerase Leu1, rapidly forming catalytically active [4Fe-4S]-containing holo-enzyme. In contrast to native SufU, its D43A variant carried a Fe/S cluster after aerobic purification, indicating that the cluster is stabilized by this mutation. Further, we show that apo-SufU is an activator of the cysteine desulfurase SufS by enhancing its activity about 40-fold in vitro. SufS-dependent formation of holo-SufU suggests that SufU functions as an Fe/S cluster scaffold protein tightly cooperating with the SufS cysteine desulfurase.
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