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AtFH binds and modulates Nfs1 kinetics in mitochondria.
NFS1 has a role in mediating the assembly of iron-sulfur clusters in mitochondria.
CpNifS was sufficient for Fe-S cluster formation in ferredoxin in the presence of cysteine and a ferrous iron salt. [CpNifS]
overexpression of this plant NifS-like protein had a pronounced effect on plant Se metabolism
CpNifS is necessary for the maturation of all plastidic Fe-S proteins and, thus, essential for plant growth
NFS1 maintains the iron sulfur clusters in proteins that are essential for protecting them from oxidative damage; inactivating NFS1 or iron sulfur clusters can trigger ferroptosis, a non-apoptotic form of cell death, in cancer cells
human NFS1 was almost fully able to complement the role of IscS in Moco biosynthesis when its specific interaction partner protein MOCS3 (show MOCS3 Proteins) from humans was also present.
The NFS1/ISD11 (show LYRM4 Proteins) complex further interacts with scaffold protein (show HOMER1 Proteins) ISCU (show ISCU Proteins) and regulator protein frataxin (show FXN Proteins), thereby forming a quaternary complex for Fe-S cluster formation.
FDX1 (show FDX1 Proteins) and FDX2 (show FDX1L Proteins) both bind NFS1 and donate electrons for iron-sulfur cluster biosynthesis.
Molecular dynamics flexible fitting of protein structures docked into the EM map of the model revealed a [FXN (show FXN Proteins)(42-210)]24.[NFS1]24.[ISD11 (show LYRM4 Proteins)]24.[ISCU (show ISCU Proteins)]24 complex, consistent with the measured 1:1:1:1 stoichiometry of its four components.
Our findings highlight that the ISD11 (show LYRM4 Proteins) R68A/R68L mutation display reduced affinity to form a stable subcomplex with NFS1, and thereby fails to prevent NFS1 aggregation resulting in impairment of the Fe-S cluster biogenesis
The data presented here show that the Isu1 suppressor mimics the frataxin (show FXN Proteins) effects on Nfs1, explaining the bypassing activity.
NFS1 binds preferentially to the D-state of ISCU (show ISCU Proteins) while mtHSP70 (show HSPA9 Proteins) binds preferentially to the D-state of ISCU (show ISCU Proteins) and HSC20 (show HSCB Proteins) binds preferentially to the S-state of ISCU (show ISCU Proteins).
the interaction of NFS1 and MOCS3 (show MOCS3 Proteins) in the cytosol of human cells, is reported.
Nfs1, the cysteine desulfurase responsible for providing sulfur for cluster formation, is required for the increased Isu stability occurring after disruption of cluster formation on or transfer from Isu
there is a mechanism that primarily dedicates m-Nfs1 to the biogenesis of mitochondrial Fe-S clusters in order to maintain cell survival
While IFN-gamma (show IFNG Proteins) alone induced Nfs1 protein instability, LPS (show TLR4 Proteins) triggered a delayed decline of Nfs1, rather involving transcriptional events or mRNA instability.
Iron-sulfur clusters are required for the function of many cellular enzymes. The proteins encoded by this gene supply inorganic sulfur to these clusters by removing the sulfur from cysteine, creating alanine in the process. This gene uses alternate in-frame translation initiation sites to generate mitochondrial forms and cytoplasmic/nuclear forms. Selection of the alternative initiation sites is determined by the cytosolic pH. The encoded proteins belong to the class-V family of pyridoxal phosphate-dependent aminotransferases. Alternatively spliced transcript variants have been described.
cysteine desulfurase NFS1
, cysteine desulfurase, (m-Nfs1)
, cysteine desulfurase
, NFS1 nitrogen fixation 1 homolog (S. cerevisiae)
, NFS1 nitrogen fixation 1 homolog
, cysteine desulfurase, mitochondrial
, nitrogen fixation 1 (S. cerevisiae, homolog)
, nitrogen-fixing bacteria S-like protein
, nitrogen fixation gene 1
, nifS-like (sic)
, nitrogen fixation gene, yeast homolog 1