The DOI matches its Crossref record; 79 of the 79 references it cites were found in a registry or an index.
Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes
Open accessAbstract
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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“Grx5 has also been found to play an important role in Fe-S cluster formation in yeast, as well as in higher eukaryotic organisms (355, 436).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [355]
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Cites
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Structure, function, and formation of biological iron-sulfur clusters
Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133518 · Cited by 1,438
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Metadata
- 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)
- Venue
- Molecular Biology of the Cell
- Published
- 2002-04
- Volume
- 13
- Issue
- 4
- Pages
- 1109-1121
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- 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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