Structure of the Yeast WD40 Domain Protein Cia1, a Component Acting Late in 
Iron-Sulfur Protein Biogenesis

Srinivasan, Vasundara; Netz, Daili J. A.; Webert, Holger; Mascarenhas, Judita; Plerik, Antonio J.; Michel, Hartmut; Lill, Roland

doi:10.1016/j.str.2007.08.009

アイテム詳細

登録内容を編集ファイル形式で保存

一時保存へ追加

このアイテムの新しいバージョンが利用可能です:
https://pure.mpg.de/pubman/item/item_2080458_3

詳細要約

公開

学術論文

Structure of the Yeast WD40 Domain Protein Cia1, a Component Acting Late in Iron-Sulfur Protein Biogenesis

MPS-Authors

/persons/resource/persons137902

Srinivasan, Vasundara
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137800

Michel, Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource

There are no locators available

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

フルテキスト (公開)

公開されているフルテキストはありません

付随資料 (公開)

There is no public supplementary material available

引用

Srinivasan, V., Netz, D. J. A., Webert, H., Mascarenhas, J., Plerik, A. J., Michel, H., & Lill, R. (2007). Structure of the Yeast WD40 Domain Protein Cia1, a Component Acting Late in Iron-Sulfur Protein Biogenesis. Structure, 15(10), 1246-1257. doi:10.1016/j.str.2007.08.009.

引用: https://hdl.handle.net/11858/00-001M-0000-0024-D872-E

要旨

The 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 A resolution. The structure folds into a beta 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.