ArticleFrontiers in molecular biosciences2017
The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX.
Article in Frontiers in molecular biosciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- Evidence the Isc iron-sulfur cluster biogenesis machinery is the source of iron for [NiFe]-cofactor biosynthesis in Escherichia coli.Scientific reports · 2024Article
- TheMicroorganisms · 2023Article
- Native mass spectrometric studies of IscSU reveal a concerted, sulfur-initiated mechanism of iron-sulfur cluster assembly.Chemical science · 2022Article
- Article
- Repair of Iron Center Proteins-A Different Class of Hemerythrin-like Proteins.Molecules (Basel, Switzerland) · 2022Review
- Protein Mutations and Stability, a Link with Disease: The Case Study of Frataxin.Biomedicines · 2022Review
- Review
- Sensing mechanisms of iron-sulfur cluster regulatory proteins elucidated using native mass spectrometry.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Native Mass Spectrometry of Iron-Sulfur Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- A Guide to Native Mass Spectrometry to determine complex interactomes of molecular machines.The FEBS journal · 2020Review
- Zinc Toxicity and Iron-Sulfur Cluster Biogenesis inApplied and environmental microbiology · 2019Article
- Generation ofBiology methods & protocols · 2019Article
- NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis.Molecules (Basel, Switzerland) · 2018Review
Corrections and comments
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Authors and funding
10 authors at 8 institutions in 4 countries.
Funding
Abstract
IscX (or YfhJ) is a protein of unknown function which takes part in the iron-sulfur cluster assembly machinery, a highly specialized and essential metabolic pathway. IscX binds to iron with low affinity and interacts with IscS, the desulfurase central to cluster assembly. Previous studies have suggested a competition between IscX and CyaY, the bacterial ortholog of frataxin, for the same binding surface of IscS. This competition could suggest a link between the two proteins with a functional significance. Using a hybrid approach based on nuclear magnetic resonance, small angle scattering and biochemical methods, we show here that IscX is a modulator of the inhibitory properties of CyaY: by competing for the same site on IscS, the presence of IscX rescues the rates of enzymatic cluster formation which are inhibited by CyaY. The effect is stronger at low iron concentrations, whereas it becomes negligible at high iron concentrations. These results strongly suggest the mechanism of the dual regulation of iron sulfur cluster assembly under the control of iron as the effector.
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