Cited by 464Redox biology and oxidative stressMetalloenzymes and iron-sulfur proteinsMitochondrial Function and Pathology

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Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes

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Rodrı́guez-Manzaneque, Marı́a Teresa, Tamarit, Jordi, Bellı́, Gemma, Ros, Joaquim, Herrero, Enrique·2002·Molecular Biology of the Cell

DOI 10.1091/mbc.01-10-0517PMC PMC102255

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Abstract

Yeast cells contain a family of three monothiol glutaredoxins: Grx3, 4, and 5. Absence of Grx5 leads to constitutive oxidative damage, exacerbating that caused by external oxidants. Phenotypic defects associated with the absence of Grx5 are suppressed by overexpression ofSSQ1 and ISA2, two genes involved in the synthesis and assembly of iron/sulfur clusters into proteins. Grx5 localizes at the mitochondrial matrix, like other proteins involved in the synthesis of these clusters, and the mature form lacks the first 29 amino acids of the translation product. Absence of Grx5 causes: 1) iron accumulation in the cell, which in turn could promote oxidative damage, and 2) inactivation of enzymes requiring iron/sulfur clusters for their activity. Reduction of iron levels in grx5 null mutants does not restore the activity of iron/sulfur enzymes, and cell growth defects are not suppressed in anaerobiosis or in the presence of disulfide reductants. Hence, Grx5 forms part of the mitochondrial machinery involved in the synthesis and assembly of iron/sulfur centers.

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Authors: Rodrı́guez-Manzaneque, M. T., Tamarit, J., Bellı́, G., Ros, J., & Herrero, E.
Affiliations: Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, 25198-Lleida, Spain
Universitat de Lleida (ES)
ORCID: Tamarit, Jordi
Bellı́, Gemma
Ros, Joaquim
Herrero, Enrique
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 2002-04
Volume: 13
Issue: 4
Pages: 1109-1121
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.01-10-0517
PMC: PMC102255
OpenAlex: W2090154662
Cited by: 464
References: 78
Citations by year: 2026: 6 · 2025: 10 · 2024: 11 · 2023: 14 · 2022: 13 · 2021: 14 · 2020: 21 · 2019: 11 · 2018: 21 · 2017: 26 · 2016: 18 · 2015: 14 · 2014: 20 · 2013: 20 · 2012: 25
FWCI: 6.37
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular Biology of the Cell (publishedVersion)
PubMed Central (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed (publishedVersion)
LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (publishedVersion, cc-by-nc-sa)
RECERCAT (Consorci de Serveis Universitaris de Catalunya) (publishedVersion, cc-by-nc-sa)
Repositori ObertUDL (University of Lleida) (publishedVersion, cc-by-nc-sa)
Funders: Generalitat de Catalunya
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords: glutaredoxin, iron-sulfur clusters, mitochondrial matrix, oxidative damage, iron accumulation, iron-sulfur cluster assembly, yeast, anaerobic conditions
MeSH terms: Amino Acid Sequence, Antifibrinolytic Agents, Iron, Iron-Sulfur Proteins, Mitochondria, Molecular Sequence Data, Mutation, Oxidation-Reduction, Oxidoreductases, Oxygen, Peptides, Plasmids, Protein Binding, Proteins, Saccharomyces cerevisiae, Time Factors, Blotting, Western, Mutagenesis, Site-Directed, Protein Structure, Tertiary, DNA, Complementary, Vitamin K 3, Glutaredoxins

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Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes

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