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Evolution and cellular function of monothiol glutaredoxins: involvement in iron-sulphur cluster assembly
Felipe Vilella1, Rui Alves, María Teresa Rodríguez-Manzaneque
1Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, Rovira Roure 44, Lleida 25198, Spain.
Comparative and Functional Genomics
|July 17, 2008
Summary
Bacterial monothiol glutaredoxins are involved in iron-sulfur cluster (ISC) assembly, interacting with key ISC proteins. Yeast Grx5 and related proteins show similar evolutionary patterns, suggesting conserved functions in ISC machinery.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Monothiol glutaredoxins, like Saccharomyces cerevisiae Grx5, are crucial for iron-sulfur cluster (ISC) synthesis.
- Bacterial proteobacteria possess Grx5-homologous monothiol glutaredoxins, suggesting conserved roles.
Purpose of the Study:
- To investigate the function of bacterial monothiol glutaredoxins in ISC assembly.
- To explore the evolutionary relationships and functional interactions of Grx5 and related proteins.
Main Methods:
- Phylogenetic profiling to predict protein function based on co-occurrence.
- Protein-protein interaction analysis using low-definition protein docking and yeast two-hybrid assays.
- Sequence comparison and cladistics to determine evolutionary origins.
Main Results:
- Phylogenetic profiles indicate bacterial monothiol glutaredoxins participate in ISC machinery.
- High co-occurrence observed between Grx5 homologues and key yeast ISC proteins (Yah1, Isa1, Isa2, Yfh1, Nfu1).
- In silico and in vivo analyses confirm physical interactions between Grx5 and yeast ISC components, notably Isa1.
Conclusions:
- Bacterial monothiol glutaredoxins are functionally integrated into the ISC assembly machinery.
- Grx5 and its bacterial homologues engage in specific interactions with other ISC proteins, highlighting conserved functional roles.
- Eukaryotic Grx3/4 types evolved from gene fusion, leading to specialized functions distinct from bacterial Grx5 homologues.
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