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    NFS1 cysteine desulfurase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850343, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1.

    During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1.
    Uzarska MA, Grochowina I, Soldek J, Jelen M, Schilke B, Marszalek J, Craig EA, Dutkiewicz R., Free PMC Article

    05/14/2022
    Compared with wild-type mitochondria, yck2 mitochondria revealed slower persulfide formation on Nfs1 consistent with a role of Yck2 in regulating mitochondrial cysteine desulfurase activity.

    Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria.
    Rocha AG, Knight SAB, Pandey A, Yoon H, Pain J, Pain D, Dancis A., Free PMC Article

    12/29/2018
    Isu is a substrate of the Lon-type protease and that it is protected from degradation by Nfs1. Nfs1 variants known to be defective in interaction with Isu were also defective in protecting Isu from degradation.

    Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulation.
    Ciesielski SJ, Schilke B, Marszalek J, Craig EA., Free PMC Article

    01/14/2017
    Mutual exclusivity of cluster assembly factor (Nfs1/Yfh1) and cluster transfer factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the transfer process during biogenesis of FeS cluster proteins.

    Overlapping binding sites of the frataxin homologue assembly factor and the heat shock protein 70 transfer factor on the Isu iron-sulfur cluster scaffold protein.
    Manicki M, Majewska J, Ciesielski S, Schilke B, Blenska A, Kominek J, Marszalek J, Craig EA, Dutkiewicz R., Free PMC Article

    01/3/2015
    The data presented here show that the Isu1 suppressor mimics the frataxin effects on Nfs1, explaining the bypassing activity.

    Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly.
    Pandey A, Gordon DM, Pain J, Stemmler TL, Dancis A, Pain D., Free PMC Article

    02/22/2014
    results show that Nfs1 adopts a higher oligomeric state in the Isd11-bound form compared to that in the free form

    The effect of the adaptor protein Isd11 on the quaternary structure of the eukaryotic cysteine desulphurase Nfs1.
    Terali K, Beavil RL, Pickersgill RW, van der Giezen M.

    12/14/2013
    Competition between Jac1 and Nfs1 for Isu binding plays an important role in transitioning the iron/Sulfur cluster biogenesis machinery.

    Binding of the chaperone Jac1 protein and cysteine desulfurase Nfs1 to the iron-sulfur cluster scaffold Isu protein is mutually exclusive.
    Majewska J, Ciesielski SJ, Schilke B, Kominek J, Blenska A, Delewski W, Song JY, Marszalek J, Craig EA, Dutkiewicz R., Free PMC Article

    12/7/2013
    Thus the Nfs1p-bound persulfide as described here represents a precursor en route to Fe-S cluster synthesis in mitochondria.

    Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria.
    Pandey A, Yoon H, Lyver ER, Dancis A, Pain D., Free PMC Article

    01/26/2013
    Whereas Nfs1p by itself was inactive, the Nfs1p.Isd11p complex formed persulfide and was active as a cysteine desulfurase. In the absence of Isd11p, Nfs1p was able to bind the substrate cysteine but failed to form a persulfide.

    Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis.
    Pandey A, Golla R, Yoon H, Dancis A, Pain D.

    01/12/2013
    Results are consistent with the existence of a mechanism to increase the stability of Isu, and thus its level, that is dependent on the presence of the cysteine desulfurase Nfs1.

    Posttranslational regulation of the scaffold for Fe-S cluster biogenesis, Isu.
    Andrew AJ, Song JY, Schilke B, Craig EA., Free PMC Article

    01/21/2010
    Isd11 acts together with Nfs1 in an early step in the biogenesis of Fe/S proteins.

    The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria.
    Adam AC, Bornhövd C, Prokisch H, Neupert W, Hell K., Free PMC Article

    01/21/2010
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