Evolution and cellular function of monothiol glutaredoxins: involvement in iron–sulphur cluster assembly
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A number of bacterial species, mostly proteobacteria, possess monothiol glutaredoxins homologous to the Saccharomyces cerevisiae mitochondrial protein Grx5, which is involved in iron–sulphur cluster synthesis. Phylogenetic profiling is used to predict that bacterial monothiol glutaredoxins also participate in the iron–sulphur cluster (ISC) assembly machinery, because their phylogenetic profiles are similar to the profiles of the bacterial homologues of yeast ISC proteins. High evolutionary co‐occurrence is observed between the Grx5 homologues and the homologues of the Yah1 ferredoxin, the scaffold proteins Isa1 and Isa2, the frataxin protein Yfh1 and the Nfu1 protein. This suggests that a specific functional interaction exists between these ISC machinery proteins. Physical interaction analyses using low‐definition protein docking predict the formation of strong and specific complexes between Grx5 and several components of the yeast ISC machinery. Two‐hybrid analysis has confirmed the in vivo interaction between Grx5 and Isa1. Sequence comparison techniques and cladistics indicate that the other two monothiol glutaredoxins of S. cerevisiae, Grx3 and Grx4, have evolved from the fusion of a thioredoxin gene with a monothiol glutaredoxin gene early in the eukaryotic lineage, leading to differential functional specialization. While bacteria do not contain these chimaeric glutaredoxins, in many eukaryotic species Grx5 and Grx3/4‐type monothiol glutaredoxins coexist in the cell. Copyright © 2004 John Wiley & Sons, Ltd.
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Grx5 plays an important role in Fe-S cluster formation in yeast and in higher eukaryotic organisms.
“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 [436]
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- Authors
- Vilella, F., Alves, R., Rodríguez‐Manzaneque, M. T., Bellí, G., Swaminathan, S., Sunnerhagen, P., & Herrero, E.
- Affiliations
- Universitat de Lleida (ES)
- University of Gothenburg (SE)
- Corresponding author
- Herrero, Enrique
- Venue
- Comparative and Functional Genomics
- Publisher
- Wiley
- Published
- 2004-05-20
- Volume
- 5
- Issue
- 4
- Pages
- 328-341
- ISSN
- 1531-6912 (ISSN-L)
- 1532-6268
- PMC
- PMC2447459
- OpenAlex
- W2128834091
- Cited by
- 54
- References
- 66
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 4 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 5 · 2013: 1 · 2012: 4
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Comparative and Functional Genomics (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Repositori ObertUDL (University of Lleida) (publishedVersion)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Spanish Ministerio de Ciencia y Tecnología (BMC2001-1213-C02-01, 2001SGR-00305, 2003-3189)
- Generalitat de Catalunya (BMC2001-1213-C02-01, 2001SGR-00305, 2003-3189)
- Swedish Research Council for Science and Technology (BMC2001-1213-C02-01, 2001SGR-00305, 2003-3189)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- monothiol glutaredoxin, NFU1, thioredoxin fusion, protein-protein interaction, phylogenetic profiling, protein docking, Saccharomyces cerevisiae, protein evolution
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