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Article

Acidic residues of yeast frataxin have an essential role in Fe-S cluster assembly.

EMBO reports - 1 Feb 2007

Foury Françoise, Pastore Annalisa, Trincal Mathieu

Abstract excerpt

Friedreich ataxia is caused by decreased levels of frataxin, a mitochondrial acidic protein that is assumed to act as chaperone in the assembly of Fe-S clusters on the scaffold Isu protein. Frataxin has the in vitro capacity to form iron-loaded multimers, which also suggests an iron storage function. It has been reported that alanine substitution of residues in an acidic ridge of yeast frataxin (Yfh1) elicits...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17186026
DOI: 10.1038/sj.embor.7400881
PMCID: PMC1796776

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Acidic residues of yeast frataxin have an essential role in Fe-S cluster assembly.PMID 17186026Read ↗

Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu.Semantic proximity Read ↗

Iron-binding activity in yeast frataxin entails a trade off with stability in the alpha1/beta1 acidic ridge region.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Turning Saccharomyces cerevisiae into a Frataxin-Independent Organism.Semantic proximity Read ↗

Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo.Semantic proximity Read ↗

Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanismSemantic proximity Read ↗

The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins.Semantic proximity Read ↗

Assembly of the iron-binding protein frataxin in Saccharomyces cerevisiae responds to dynamic changes in mitochondrial iron influx and stress level.Semantic proximity Read ↗

Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly.Semantic proximity Read ↗

Frataxin: a protein in search for a function.Semantic proximity Read ↗

The structure and function of frataxin.Semantic proximity Read ↗

Frataxin-bypassing Isu1: characterization of the bypass activity in cells and mitochondria.Semantic proximity Read ↗

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