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Binding of IscU and TusA to different but competing sites of IscS influences the activity of IscS and directs sulfur to the respective biomolecular synthesis pathway

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Title: Binding of IscU and TusA to different but competing sites of IscS influences the activity of IscS and directs sulfur to the respective biomolecular synthesis pathway
Authors: Paolo Olivieri, Moritz Klabes, Jason C. Crack, Angelika Lehmann, Sophie P. Bennett, Nick E. Le Brun, Silke Leimkühler
Source: Microbiology Spectrum, Vol 12, Iss 8 (2024)
Publisher Information: American Society for Microbiology, 2024.
Publication Year: 2024
Collection: LCC:Microbiology
Subject Terms: IscS, Fe-S cluster, iron, sulfur, cysteine desulfurase, Microbiology, QR1-502
More Details: ABSTRACT All sulfur transfer pathways generally have in common an l-cysteine desulfurase as the initial sulfur-mobilizing enzyme, which serves as a sulfur donor for the biosynthesis of numerous sulfur-containing biomolecules in the cell. In Escherichia coli, the housekeeping l-cysteine desulfurase IscS functions as a hub for sulfur transfer through interactions with several partner proteins, which bind at different sites on IscS. So far, the interaction sites of IscU, Fdx, CyaY, and IscX involved in iron sulfur (Fe-S) cluster assembly, TusA, required for molybdenum cofactor biosynthesis and mnm5s2U34 transfer RNA (tRNA) modifications, and ThiI, involved in both the biosynthesis of thiamine and s4U8 tRNA modifications, have been mapped. Previous studies have suggested that IscS partner proteins bind only one at a time, with the exception of Fe-S cluster assembly, which involves the formation of a ternary complex involving IscS, IscU, and one of CyaY, Fdx, or IscX. Here, we show that the affinity of TusA for IscS is similar to but lower than that of IscU and that these proteins compete for binding to IscS. We show that heterocomplexes involving the IscS dimer and single IscU and TusA molecules are readily formed and that binding of both TusA and IscU to IscS affects its l-cysteine desulfurase activity. A model is proposed in which the delivery of sulfur to different sulfur-requiring pathways is controlled by sulfur acceptor protein levels, IscS-binding affinities, and acceptor protein-modulated IscS desulfurase activity.IMPORTANCEIron-sulfur clusters are evolutionarily ancient prosthetic groups. The housekeeping l-cysteine desulfurase IscS functions as a central core for sulfur transfer through interactions with several partner proteins, which bind at different sites on each IscS monomer with different affinities and partially overlapping binding sites. We show that heterocomplexes involving the IscS dimer and single IscU and TusA molecules at each site of the dimer are formed, thereby influencing the activity of IscS.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2165-0497
Relation: https://doaj.org/toc/2165-0497
DOI: 10.1128/spectrum.00949-24
Access URL: https://doaj.org/article/0f7a42399e5d4ba7bfb2e37cbde98729
Accession Number: edsdoj.0f7a42399e5d4ba7bfb2e37cbde98729
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  Data: Binding of IscU and TusA to different but competing sites of IscS influences the activity of IscS and directs sulfur to the respective biomolecular synthesis pathway
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  Data: <searchLink fieldCode="AR" term="%22Paolo+Olivieri%22">Paolo Olivieri</searchLink><br /><searchLink fieldCode="AR" term="%22Moritz+Klabes%22">Moritz Klabes</searchLink><br /><searchLink fieldCode="AR" term="%22Jason+C%2E+Crack%22">Jason C. Crack</searchLink><br /><searchLink fieldCode="AR" term="%22Angelika+Lehmann%22">Angelika Lehmann</searchLink><br /><searchLink fieldCode="AR" term="%22Sophie+P%2E+Bennett%22">Sophie P. Bennett</searchLink><br /><searchLink fieldCode="AR" term="%22Nick+E%2E+Le+Brun%22">Nick E. Le Brun</searchLink><br /><searchLink fieldCode="AR" term="%22Silke+Leimkühler%22">Silke Leimkühler</searchLink>
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  Data: Microbiology Spectrum, Vol 12, Iss 8 (2024)
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  Data: American Society for Microbiology, 2024.
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  Data: ABSTRACT All sulfur transfer pathways generally have in common an l-cysteine desulfurase as the initial sulfur-mobilizing enzyme, which serves as a sulfur donor for the biosynthesis of numerous sulfur-containing biomolecules in the cell. In Escherichia coli, the housekeeping l-cysteine desulfurase IscS functions as a hub for sulfur transfer through interactions with several partner proteins, which bind at different sites on IscS. So far, the interaction sites of IscU, Fdx, CyaY, and IscX involved in iron sulfur (Fe-S) cluster assembly, TusA, required for molybdenum cofactor biosynthesis and mnm5s2U34 transfer RNA (tRNA) modifications, and ThiI, involved in both the biosynthesis of thiamine and s4U8 tRNA modifications, have been mapped. Previous studies have suggested that IscS partner proteins bind only one at a time, with the exception of Fe-S cluster assembly, which involves the formation of a ternary complex involving IscS, IscU, and one of CyaY, Fdx, or IscX. Here, we show that the affinity of TusA for IscS is similar to but lower than that of IscU and that these proteins compete for binding to IscS. We show that heterocomplexes involving the IscS dimer and single IscU and TusA molecules are readily formed and that binding of both TusA and IscU to IscS affects its l-cysteine desulfurase activity. A model is proposed in which the delivery of sulfur to different sulfur-requiring pathways is controlled by sulfur acceptor protein levels, IscS-binding affinities, and acceptor protein-modulated IscS desulfurase activity.IMPORTANCEIron-sulfur clusters are evolutionarily ancient prosthetic groups. The housekeeping l-cysteine desulfurase IscS functions as a central core for sulfur transfer through interactions with several partner proteins, which bind at different sites on each IscS monomer with different affinities and partially overlapping binding sites. We show that heterocomplexes involving the IscS dimer and single IscU and TusA molecules at each site of the dimer are formed, thereby influencing the activity of IscS.
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        Value: 10.1128/spectrum.00949-24
    Languages:
      – Text: English
    Subjects:
      – SubjectFull: IscS
        Type: general
      – SubjectFull: Fe-S cluster
        Type: general
      – SubjectFull: iron
        Type: general
      – SubjectFull: sulfur
        Type: general
      – SubjectFull: cysteine desulfurase
        Type: general
      – SubjectFull: Microbiology
        Type: general
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      – TitleFull: Binding of IscU and TusA to different but competing sites of IscS influences the activity of IscS and directs sulfur to the respective biomolecular synthesis pathway
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