Structure of the Yeast WD40 Domain Protein Cia1, a Component Acting Late in Iron-Sulfur Protein Biogenesis
| Autor: | Vasundara Srinivasan, Judita Mascarenhas, Hartmut Michel, Daili J. A. Netz, Antonio J. Pierik, Roland Lill, Holger Webert |
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| Rok vydání: | 2007 |
| Předmět: |
Iron-Sulfur Proteins
Saccharomyces cerevisiae Proteins PROTEINS Molecular Sequence Data Protein domain Saccharomyces cerevisiae Cell Cycle Proteins Sequence alignment Crystallography X-Ray Structure-Activity Relationship Structural Biology Animals Humans Amino Acid Sequence Cloning Molecular Cell Cycle Protein Molecular Biology Peptide sequence biology biology.organism_classification Yeast Protein tertiary structure Protein Structure Tertiary Metallochaperones Biochemistry Carrier Proteins Sequence Alignment Biogenesis |
| Zdroj: | Structure. 15:1246-1257 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2007.08.009 |
| Popis: | SummaryThe WD40-repeat protein Cia1 is an essential, conserved member of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery in eukaryotes. Here, we report the crystal structure of Saccharomyces cerevisiae Cia1 to 1.7 Å resolution. The structure folds into a β propeller with seven blades pseudo symmetrically arranged around a central axis. Structure-based sequence alignment of Cia1 proteins shows that the WD40 propeller core elements are highly conserved. Site-directed mutagenesis of amino acid residues in loop regions with high solvent accessibility identified that the conserved top surface residue R127 performs a critical function: the R127 mutant cells grew slowly and were impaired in cytosolic Fe/S protein assembly. Human Ciao1, which reportedly interacts with the Wilms' tumor suppressor, WT1, is structurally similar to yeast Cia1. We show that Ciao1 can functionally replace Cia1 and support cytosolic Fe/S protein biogenesis. Hence, our structural and biochemical studies indicate the conservation of Cia1 function in eukaryotes. |
| Databáze: | OpenAIRE |
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