ArticleProceedings of the National Academy of Sciences of the United States of America2012
Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Structural heterogeneity of iron-sulfur cluster scaffold protein IscU: Metamorphic or partially folded?Structural dynamics (Melville, N.Y.) · 2026Review
- Slowly exchanging bound states of SARS-CoV-2 3CLStructural dynamics (Melville, N.Y.) · 2026Article
- Intricacies in iron-sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme specificity.RSC chemical biology · 2026Review
- Systematic genome-wide mapping of host determinants of bacteriophage infectivity.Cell systems · 2025Article
- Plant-specific cochaperone SSR1 affects root elongation by modulating the mitochondrial iron-sulfur cluster assembly machinery.PLoS genetics · 2025Article
- The conformational landscape of fold-switcher KaiB is tuned to the circadian rhythm timescale.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Analysis of Reconstituted Tripartite Complex Supports Avidity-based Recruitment of Hsp70 by Substrate Bound J-domain Protein.Journal of molecular biology · 2023Article
- Native mass spectrometric studies of IscSU reveal a concerted, sulfur-initiated mechanism of iron-sulfur cluster assembly.Chemical science · 2022Article
- Article
- Iron Insertion at the Assembly Site of the ISCU Scaffold Protein Is a Conserved Process Initiating Fe-S Cluster Biosynthesis.Journal of the American Chemical Society · 2022Article
- Article
- Spectroscopic and functional characterization of the [2Fe-2S] scaffold protein Nfu from Synechocystis PCC6803.Biochimie · 2022Article
- Interaction of client-the scaffold on which FeS clusters are build-with J-domain protein Hsc20 and its evolving Hsp70 partners.Frontiers in molecular biosciences · 2022Review
- The interactions of molecular chaperones with client proteins: why are they so weak?The Journal of biological chemistry · 2021Review
- Iron-Sulfur Cluster Biogenesis as a Critical Target in Cancer.Antioxidants (Basel, Switzerland) · 2021Review
- Metamorphic proteins: the Janus proteins of structural biology.Open biology · 2021Article
- Analysis of differential expression of hypoxia-inducible microRNA-210 gene targets in mild and severe preeclamptic patients.Non-coding RNA research · 2021Article
- The cytotoxicity of gallium maltolate in glioblastoma cells is enhanced by metformin through combined action on mitochondrial complex 1.Oncotarget · 2020Article
- Molecular Mechanism of ISC Iron-Sulfur Cluster Biogenesis Revealed by High-Resolution Native Mass Spectrometry.Journal of the American Chemical Society · 2020Article
- Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity.Biochimie · 2018Article
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3 authors.
Funding
Abstract
The scaffold protein for iron-sulfur cluster assembly, apo-IscU, populates two interconverting conformational states, one disordered (D) and one structured (S) as revealed by extensive NMR assignments. At pH 8 and 25 °C, approximately 70% of the protein is S, and the lifetimes of the states are 1.3 s (S) and 0.50 s (D). Zn(II) and Fe(II) each bind and stabilize structured (S-like) states. Single amino acid substitutions at conserved residues were found that shift the equilibrium toward either the S or the D state. Cluster assembly takes place in the complex between IscU and the cysteine desulfurase, IscS, and our NMR studies demonstrate that IscS binds preferentially the D form of apo-IscU. The addition of 10% IscS to IscU was found to greatly increase H/D exchange at protected amides of IscU, to increase the rate of the S → D reaction, and to decrease the rate of the D → S reaction. In the saturated IscU:IscS complex, IscU is largely disordered. In vitro cluster assembly reactions provided evidence for the functional importance of the S&lrarr2;D equilibrium. IscU variants that favor the S state were found to undergo a lag phase, not observed with the wild type, that delayed cluster assembly; variants that favor the D state were found to assemble less stable clusters at an intermediate rate without the lag. It appears that IscU has evolved to exist in a disordered conformational state that is the initial substrate for the desulfurase and to convert to a structured state that stabilizes the cluster once it is assembled.
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