ISU1 iron-binding protein ISU1 [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Official Symbol: ISU1
Official Full Name: iron-binding protein ISU1
Primary source: SGD:S000006056
Locus tag: YPL135W
See related: AllianceGenome:SGD:S000006056; FungiDB:YPL135W; VEuPathDB:YPL135W
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: NUA1
Summary: Enables ATPase activator activity; ferrous iron binding activity; and zinc ion binding activity. Involved in intracellular iron ion homeostasis; iron-sulfur cluster assembly; and tRNA wobble uridine modification. Located in mitochondrial matrix. Used to study mitochondrial myopathy. Orthologous to human ISCU (iron-sulfur cluster assembly enzyme). [provided by Alliance of Genome Resources, Dec 2024]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

See ISU1 in Genome Data Viewer

Location:: chromosome: XVI

Exon count:: 1

Sequence:: Chromosome: XVI; NC_001148.4 (297553..298050)

Chromosome XVI - NC_001148.4 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001148.4

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Characteristics of the Isu1 C-terminus in relation to [2Fe-2S] cluster assembly and ISCU Myopathy.
Title: Characteristics of the Isu1 C-terminus in relation to [2Fe-2S] cluster assembly and ISCU Myopathy.
In the absence of Yfh1, Isu1 was found to exist in two forms, one mostly monomeric with limited tendency to dimerize, distinct structural features suggest that in physiological conditions the zinc-regulated abundance of monomeric vs. oligomeric Isu1 yields [Yfh1].[Isu1] complexes with different Isu1 configurations that afford unique functional properties for Fe-S cluster assembly and delivery.
Title: Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe-S cluster assembly centers.
Proteomic and metabolomic comparisons revealed that the xylose-metabolizing mutant strains exhibit altered metabolic pathways relative to the parental strain when grown in xylose. Further analyses revealed that interacting mutations in HOG1 and ISU1 unexpectedly elevated mitochondrial respiratory proteins and enabled rapid aerobic respiration of xylose and other non-fermentable carbon substrates.
Title: Directed Evolution Reveals Unexpected Epistatic Interactions That Alter Metabolic Regulation and Enable Anaerobic Xylose Use by Saccharomyces cerevisiae.
Isu is a substrate of the Lon-type protease and that it is protected from degradation by Nfs1, the sulfur donor for Fe-S cluster assembly, as well as by Jac1, the J-protein Hsp70 cochaperone that functions in cluster transfer from Isu. Nfs1 and Jac1 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.
Studied the structure and dynamics of the yeast Isu1-Jac1 complex.
Title: Molecular modeling of the binding modes of the iron-sulfur protein to the Jac1 co-chaperone from Saccharomyces cerevisiae by all-atom and coarse-grained approaches.
The eukaryotic forms are critical for Fe-S cluster assembly whereas prokaryotic forms are more dispensable. We found that a key to this difference is a single amino acid in the scaffold protein Isu1 at position 141.
Title: Turning Saccharomyces cerevisiae into a Frataxin-Independent Organism.
Fe/S cluster synthesis on Isu1 requires the ferredoxin Yah1
Title: Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin.
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.
In frataxin-deleted strains expressing the bypass mutant Isu1, cell growth and iron homeostasis are restored to close to normal.
Title: Frataxin-bypassing Isu1: characterization of the bypass activity in cells and mitochondria.
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.

Submit: New GeneRIF Correction See all GeneRIFs (21)

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables 2 iron, 2 sulfur cluster binding	IBA Inferred from Biological aspect of Ancestor more info
enables 2 iron, 2 sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables ATPase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables ferrous iron binding	IBA Inferred from Biological aspect of Ancestor more info
enables ferrous iron binding	IDA Inferred from Direct Assay more info	PubMed
enables iron ion binding	IDA Inferred from Direct Assay more info	PubMed
enables iron ion binding	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 zinc ion binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in intracellular iron ion homeostasis	IBA Inferred from Biological aspect of Ancestor more info
involved_in intracellular iron ion homeostasis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in iron-sulfur cluster assembly	IEA Inferred from Electronic Annotation more info
involved_in iron-sulfur cluster assembly	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within iron-sulfur cluster assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in iron-sulfur cluster assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in tRNA wobble uridine modification	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
is_active_in mitochondrial matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: iron-binding protein ISU1

NP_015190.1

Conserved protein of the mitochondrial matrix; performs a scaffolding function during assembly of iron-sulfur clusters, interacts physically and functionally with yeast frataxin (Yfh1p); ISU1 has a paralog, ISU2, that arose from the whole genome duplication; isu1 isu2 double mutant is inviable; human homolog ISCU implicated in mitochondrial myopathy, can complement isu1 isu2 double mutant