The effect of the adaptor protein Isd11 on the quaternary structure of the eukaryotic cysteine desulphurase Nfs1

Biochem Biophys Res Commun. 2013 Oct 18;440(2):235-40. doi: 10.1016/j.bbrc.2013.09.039. Epub 2013 Sep 14.


Small inorganic assemblies of alternating ferrous/ferric iron and sulphide ions, so-called iron-sulphur (Fe-S) clusters, are possibly nature's most ancient prosthetic groups. One of the early actors in Fe-S cluster biosynthesis is a protein complex composed of a cysteine desulphurase, Nfs1, and its functional binding partner, Isd11. Although the essential function of Nfs1·Isd11 in the liberation of elemental sulphur from free cysteine is well established, little is known about its structure. Here, we provide evidence that shows Isd11 has a profound effect on the oligomeric state of Nfs1.

Keywords: Iron–sulphur (Fe–S) cluster assembly; Isd11; Mitochondria; Nfs1; Saccharomyces cerevisiae.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Circular Dichroism
  • Iron-Sulfur Proteins / chemistry*
  • Mitochondrial Proteins / chemistry*
  • Mitochondrial Proteins / metabolism*
  • Models, Molecular
  • Protein Structure, Quaternary*
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Spectrophotometry, Ultraviolet
  • Structural Homology, Protein
  • Sulfurtransferases / chemistry*


  • Iron-Sulfur Proteins
  • Isd11 protein, S cerevisiae
  • Mitochondrial Proteins
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Sulfurtransferases
  • NFS1 protein, S cerevisiae