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Molecular Details of the Frataxin-Scaffold Interaction during Mitochondrial Fe-S Cluster Assembly.
Campbell, Courtney J; Pall, Ashley E; Naik, Akshata R; Thompson, Lindsey N; Stemmler, Timothy L.
Afiliación
  • Campbell CJ; Department of Pharmaceutical Sciences, Wayne State University, Detroit, MI 48201, USA.
  • Pall AE; Department of Pharmaceutical Sciences, Wayne State University, Detroit, MI 48201, USA.
  • Naik AR; Department of Pharmaceutical Sciences, Wayne State University, Detroit, MI 48201, USA.
  • Thompson LN; Department of Pharmaceutical Sciences, Wayne State University, Detroit, MI 48201, USA.
  • Stemmler TL; Department of Pharmaceutical Sciences, Wayne State University, Detroit, MI 48201, USA.
Int J Mol Sci ; 22(11)2021 Jun 02.
Article en En | MEDLINE | ID: mdl-34199378
Iron-sulfur clusters are essential to almost every life form and utilized for their unique structural and redox-targeted activities within cells during many cellular pathways. Although there are three different Fe-S cluster assembly pathways in prokaryotes (the NIF, SUF and ISC pathways) and two in eukaryotes (CIA and ISC pathways), the iron-sulfur cluster (ISC) pathway serves as the central mechanism for providing 2Fe-2S clusters, directly and indirectly, throughout the entire cell in eukaryotes. Proteins central to the eukaryotic ISC cluster assembly complex include the cysteine desulfurase, a cysteine desulfurase accessory protein, the acyl carrier protein, the scaffold protein and frataxin (in humans, NFS1, ISD11, ACP, ISCU and FXN, respectively). Recent molecular details of this complex (labeled NIAUF from the first letter from each ISC protein outlined earlier), which exists as a dimeric pentamer, have provided real structural insight into how these partner proteins arrange themselves around the cysteine desulfurase, the core dimer of the (NIAUF)2 complex. In this review, we focus on both frataxin and the scaffold within the human, fly and yeast model systems to provide a better understanding of the biophysical characteristics of each protein alone and within the FXN/ISCU complex as it exists within the larger NIAUF construct. These details support a complex dynamic interaction between the FXN and ISCU proteins when both are part of the NIAUF complex and this provides additional insight into the coordinated mechanism of Fe-S cluster assembly.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Azufre / Proteínas de Unión a Hierro / Hierro / Proteínas Hierro-Azufre Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Azufre / Proteínas de Unión a Hierro / Hierro / Proteínas Hierro-Azufre Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza