Maturation of cytosolic and nuclear iron-sulfur proteins

Trends Cell Biol. 2014 May;24(5):303-12. doi: 10.1016/j.tcb.2013.11.005. Epub 2013 Dec 3.

Abstract

Eukaryotic cells contain numerous cytosolic and nuclear iron-sulfur (Fe/S) proteins that perform key functions in metabolic catalysis, iron regulation, protein translation, DNA synthesis, and DNA repair. Synthesis of Fe/S clusters and their insertion into apoproteins are essential for viability and are conserved in eukaryotes. The process is catalyzed in two major steps by the CIA (cytosolic iron-sulfur protein assembly) machinery encompassing nine known proteins. First, a [4Fe-4S] cluster is assembled on a scaffold complex. This step requires a sulfur-containing compound from mitochondria and reducing equivalents from an electron transfer chain. Second, the Fe/S cluster is transferred from the scaffold to specific apoproteins by the CIA targeting complex. This review summarizes our molecular knowledge on CIA protein function during the assembly process.

Keywords: DNA helicase; DNA polymerases; Iron–sulfur cluster; genome integrity; iron regulation; mitochondrial ISC system.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Binding Sites
  • Cytosol / metabolism
  • Genomic Instability
  • Humans
  • Iron-Sulfur Proteins / biosynthesis*
  • Iron-Sulfur Proteins / physiology
  • Mitochondria / metabolism
  • Molecular Chaperones / physiology
  • Nuclear Proteins / biosynthesis
  • Nuclear Proteins / physiology
  • Protein Biosynthesis
  • Protein Folding

Substances

  • Iron-Sulfur Proteins
  • Molecular Chaperones
  • Nuclear Proteins