Cited by 54Metalloenzymes and iron-sulfur proteinsRedox biology and oxidative stressEnzyme Structure and Function

Evolution and cellular function of monothiol glutaredoxins: involvement in iron–sulphur cluster assembly

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Vilella, Felipe, Alves, Rui, Rodríguez‐Manzaneque, María Teresa, Bellí, Gemma, Swaminathan, Swarna, Sunnerhagen, Per, Herrero, Enrique·2004·Comparative and Functional Genomics

Abstract

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
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
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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