Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis
- 29 August 2010
- journal article
- Published by Springer Nature in Nature Chemical Biology
- Vol. 6 (10), 758-765
- https://doi.org/10.1038/nchembio.432
Abstract
Iron-sulfur clusters are essential components of many proteins and are assembled in a hierarchical pathway. Tah18 is a diflavin reductase that transfers electrons to the [2Fe-2S] cluster of Dre2 in an early step of iron-sulfur cluster biogenesis in the cytoplasm of eukaryotes.Keywords
This publication has 50 references indexed in Scilit:
- Crucial Role of Conserved Cysteine Residues in the Assembly of Two Iron−Sulfur Clusters on the CIA Protein Nar1Biochemistry, 2009
- Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and DiseasesAnnual Review of Biochemistry, 2008
- A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein BiogenesisJournal of Biological Chemistry, 2008
- Structure of the Yeast WD40 Domain Protein Cia1, a Component Acting Late in Iron-Sulfur Protein BiogenesisStructure, 2007
- A versatile toolbox for PCR‐based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettesYeast, 2004
- A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteinsProceedings of the National Academy of Sciences, 2000
- Cloning and Characterization of a Novel Human Dual Flavin ReductaseJournal of Biological Chemistry, 2000
- The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteinsThe EMBO Journal, 1999
- Role of Acidic Residues in the Interaction of NADPH-Cytochrome P450 Oxidoreductase with Cytochrome P450 and Cytochrome cJournal of Biological Chemistry, 1995
- [1] Getting started with yeastMethods in Enzymology, 1991