NFS1 cysteine desulfurase [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: NFS1
Official Full Name: cysteine desulfurase
Primary source: SGD:S000000522
Locus tag: YCL017C
See related: AllianceGenome:SGD:S000000522; FungiDB:YCL017C; VEuPathDB:YCL017C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: SPL1
Summary: Enables cysteine desulfurase activity. Involved in cellular iron ion homeostasis; iron-sulfur cluster assembly; and tRNA modification. Located in mitochondrion and nucleus. Part of L-cysteine desulfurase complex. Human ortholog(s) of this gene implicated in combined oxidative phosphorylation deficiency. Orthologous to human NFS1 (NFS1 cysteine desulfurase). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See NFS1 in Genome Data Viewer

Location:: chromosome: III

Exon count:: 1

Sequence:: Chromosome: III; NC_001135.5 (92777..94270, complement)

Chromosome III - NC_001135.5 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001135.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1.
Title: During FeS cluster biogenesis, ferredoxin and frataxin use overlapping binding sites on yeast cysteine desulfurase Nfs1.
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.
Title: Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria.
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.
Title: Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulation.
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.
Title: 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.
The data presented here show that the Isu1 suppressor mimics the frataxin effects on Nfs1, explaining the bypassing activity.
Title: 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.
results show that Nfs1 adopts a higher oligomeric state in the Isd11-bound form compared to that in the free form
Title: The effect of the adaptor protein Isd11 on the quaternary structure of the eukaryotic cysteine desulphurase Nfs1.
Competition between Jac1 and Nfs1 for Isu binding plays an important role in transitioning the iron/Sulfur cluster biogenesis machinery.
Title: Binding of the chaperone Jac1 protein and cysteine desulfurase Nfs1 to the iron-sulfur cluster scaffold Isu protein is mutually exclusive.
Thus the Nfs1p-bound persulfide as described here represents a precursor en route to Fe-S cluster synthesis in mitochondria.
Title: Identification of a Nfs1p-bound persulfide intermediate in Fe-S cluster synthesis by intact mitochondria.
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.
Title: Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis.
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.
Title: Posttranslational regulation of the scaffold for Fe-S cluster biogenesis, Isu.

Submit: New GeneRIF Correction See all GeneRIFs (11)

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables cysteine desulfurase activity	IBA Inferred from Biological aspect of Ancestor more info
enables cysteine desulfurase activity	IDA Inferred from Direct Assay more info	PubMed
enables cysteine desulfurase activity	IEA Inferred from Electronic Annotation more info
enables iron-sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables pyridoxal phosphate binding	IEA Inferred from Electronic Annotation more info
enables transferase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in [2Fe-2S] cluster assembly	IEA Inferred from Electronic Annotation more info
involved_in intracellular iron ion homeostasis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in iron-sulfur cluster assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in iron-sulfur cluster assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in iron-sulfur cluster assembly	IEA Inferred from Electronic Annotation more info
involved_in iron-sulfur cluster assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitochondrial tRNA thio-modification	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in tRNA processing	IEA Inferred from Electronic Annotation more info
involved_in tRNA thio-modification	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in tRNA wobble uridine modification	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of L-cysteine desulfurase complex	IPI Inferred from Physical Interaction more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IMP Inferred from Mutant Phenotype more info	PubMed

General protein information

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Preferred Names: cysteine desulfurase

NP_009912.2

EC 2.8.1.7

Cysteine desulfurase involved in iron-sulfur cluster biogenesis; required for thio-modification of mitochondrial and cytoplasmic tRNAs; involved in DNA damage response by providing iron-sulfur cluster cofactors for DNA repair enzymes; essential protein located predominantly in mitochondria

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001135.5 Reference assembly

Range

92777..94270 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178664.1 → NP_009912.2 TPA: cysteine desulfurase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009912.2

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQZ7, P25374

UniProtKB/TrEMBL

A6ZTG9, B5VET7, C7GQK3, C8Z470, G2WA05

Conserved Domains (1) summary

cl18945
Location:99 → 497

AAT_I; Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the ...