Expression, purification, and characterization of an iron chaperon protein CyaY from Acidithiobacillus ferrooxidans

Curr Microbiol. 2011 Mar;62(3):733-8. doi: 10.1007/s00284-010-9775-2.

Abstract

CyaY is the bacterial homolog of frataxin, proposed to be involved in the assembly of iron-sulfur clusters. While, the physiological iron donor for the iron-sulfur clusters assembly remains controversial. In this study, the gene of CyaY from Acidithiobacillus ferrooxidans was cloned and expressed in Escherichia coli, the protein was purified by one-step affinity chromatography to homogeneity. The CyaY protein can bind ferric iron and serve as an iron donor for the biogenesis of iron-sulfur clusters on the scaffold protein IscU in the presence of IscS and L-cysteine in vitro.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acidithiobacillus / enzymology*
  • Acidithiobacillus / genetics
  • Amino Acid Sequence
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Chromatography, Affinity
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Ferric Compounds / metabolism
  • Iron / metabolism
  • Models, Molecular
  • Molecular Chaperones / genetics
  • Molecular Chaperones / isolation & purification
  • Molecular Chaperones / metabolism*
  • Molecular Sequence Data
  • Protein Binding
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • Ferric Compounds
  • Molecular Chaperones
  • Recombinant Proteins
  • Iron