N-terminal domains mediate [2Fe-2S] cluster transfer from glutaredoxin-3 to anamorsin

Nat Chem Biol. 2015 Oct;11(10):772-8. doi: 10.1038/nchembio.1892. Epub 2015 Aug 24.


In eukaryotes, cytosolic monothiol glutaredoxins are proteins implicated in intracellular iron trafficking and sensing via their bound [2Fe-2S] clusters. We define a new role of human cytosolic monothiol glutaredoxin-3 (GRX3) in transferring its [2Fe-2S] clusters to human anamorsin, a physical and functional protein partner of GRX3 in the cytosol, whose [2Fe-2S] cluster-bound form is involved in the biogenesis of cytosolic and nuclear Fe-S proteins. Specific protein recognition between the N-terminal domains of the two proteins is the mandatory requisite to promote the [2Fe-2S] cluster transfer from GRX3 to anamorsin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoproteins / chemistry
  • Apoproteins / metabolism
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cytosol / metabolism
  • Escherichia coli / genetics
  • Humans
  • Intracellular Signaling Peptides and Proteins / chemistry
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Iron / metabolism*
  • Iron-Sulfur Proteins / chemistry
  • Iron-Sulfur Proteins / genetics
  • Iron-Sulfur Proteins / metabolism*
  • Models, Biological
  • Molecular Docking Simulation
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Protein Transport


  • Apoproteins
  • CIAPIN1 protein, human
  • Carrier Proteins
  • GLRX3 protein, human
  • Intracellular Signaling Peptides and Proteins
  • Iron-Sulfur Proteins
  • Iron