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

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

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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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  1. Gietz R.D., 1988, Gene, 74, 3065
  2. Pon L., 1991, The Molecular and Cellular Biology of the Yeast Saccharomyces, 1, 333

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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)
ORCID
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
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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