ArticleThe Journal of biological chemistry2013
Physical and functional interactions of a monothiol glutaredoxin and an iron sulfur cluster carrier protein with the sulfur-donating radical S-adenosyl-L-methionine enzyme MiaB.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- Monothiol glutaredoxins in microbial iron metabolism: From iron-sulfur cluster trafficking to iron-dependent regulation.Advances in microbial physiology · 2026Review
- Essentiality of theInternational journal of molecular sciences · 2023Article
- Monothiol Glutaredoxin Is Essential for Oxidative Stress Protection and Virulence in Pseudomonas aeruginosa.Applied and environmental microbiology · 2023Article
- Review
- A-Type Carrier Proteins Are Involved in [4Fe-4S] Cluster Insertion into the RadicalJournal of bacteriology · 2021Article
- Quantitative Genetic Screens for Mapping Bacterial Pathways and Functional Networks.Methods in molecular biology (Clifton, N.J.) · 2021Article
- First Step in Catalysis of the RadicalJournal of the American Chemical Society · 2020Article
- Is There a Role for Glutaredoxins and BOLAs in the Perception of the Cellular Iron Status in Plants?Frontiers in plant science · 2019Article
- The ErpA/NfuA complex builds an oxidation-resistant Fe-S cluster delivery pathway.The Journal of biological chemistry · 2018Article
- Characterization of Glutaredoxin Fe-S Cluster-Binding Interactions Using Circular Dichroism Spectroscopy.Methods in enzymology · 2018Article
- Biochemical Approaches for Understanding Iron-Sulfur Cluster Regeneration in Escherichia coli Lipoyl Synthase During Catalysis.Methods in enzymology · 2018Article
- Destruction and reformation of an iron-sulfur cluster during catalysis by lipoyl synthase.Science (New York, N.Y.) · 2017Article
- The Escherichia coli BolA Protein IbaG Forms a Histidine-Ligated [2Fe-2S]-Bridged Complex with Grx4.Biochemistry · 2016Article
- Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins.eLife · 2016Article
- Article
- Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM).Biochimica et biophysica acta · 2015Review
- How Is Fe-S Cluster Formation Regulated?Annual review of microbiology · 2015Review
- Structure-to-function relationships of bacterial translocator protein (TSPO): a focus on Pseudomonas.Frontiers in microbiology · 2014Article
- The iron-sulfur cluster assembly machineries in plants: current knowledge and open questions.Frontiers in plant science · 2013Article
- Glutaredoxins are essential for stress adaptation in the cyanobacterium Synechocystis sp. PCC 6803.Frontiers in plant science · 2013Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The biosynthesis of iron sulfur (FeS) clusters, their trafficking from initial assembly on scaffold proteins via carrier proteins to final incorporation into FeS apoproteins, is a highly coordinated process enabled by multiprotein systems encoded in iscRSUAhscBAfdx and sufABCDSE operons in Escherichia coli. Although these systems are believed to encode all factors required for initial cluster assembly and transfer to FeS carrier proteins, accessory factors such as monothiol glutaredoxin, GrxD, and the FeS carrier protein NfuA are located outside of these defined systems. These factors have been suggested to function both as shuttle proteins acting to transfer clusters between scaffold and carrier proteins and in the final stages of FeS protein assembly by transferring clusters to client FeS apoproteins. Here we implicate both of these factors in client protein interactions. We demonstrate specific interactions between GrxD, NfuA, and the methylthiolase MiaB, a radical S-adenosyl-L-methionine-dependent enzyme involved in the maturation of a subset of tRNAs. We show that GrxD and NfuA physically interact with MiaB with affinities compatible with an in vivo function. We furthermore demonstrate that NfuA is able to transfer its cluster in vitro to MiaB, whereas GrxD is unable to do so. The relevance of these interactions was demonstrated by linking the activity of MiaB with GrxD and NfuA in vivo. We observe a severe defect in in vivo MiaB activity in cells lacking both GrxD and NfuA, suggesting that these proteins could play complementary roles in maturation and repair of MiaB.
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