Mechanistic characterization of sulfur transfer from cysteine desulfurase SufS to the iron-sulfur scaffold SufU in Bacillus subtilis

FEBS Lett. 2011 Feb 4;585(3):465-70. doi: 10.1016/j.febslet.2011.01.005. Epub 2011 Jan 12.

Abstract

Iron-sulfur cluster biosynthesis in Gram-positive bacteria is mediated by the SUF system. The transfer of sulfide from the cysteine desulfurase SufS to the scaffold protein SufU is one of the first steps within the assembly process. In this study, we analyzed the interaction between Bacillus subtilis SufS and its scaffold SufU. The activity of SufS represents a Ping-Pong mechanism leading to successive sulfur loading of the conserved cysteine residues in SufU. Cysteine 41 of SufU is shown to be essential for receiving sulfide from SufS, while cysteines 66 and 128 are needed for SufS/SufU interaction. In conclusion, we present the first step-by-step model for loading of the essential scaffold component SufU by its sulfur donor SufS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Bacillus subtilis / enzymology
  • Bacillus subtilis / metabolism*
  • Biocatalysis*
  • Carbon-Sulfur Lyases / chemistry*
  • Carbon-Sulfur Lyases / metabolism*
  • Catalytic Domain
  • Cysteine / metabolism
  • Gram-Positive Bacteria / enzymology
  • Gram-Positive Bacteria / metabolism
  • Iron / chemistry
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / metabolism*
  • Kinetics
  • Models, Molecular
  • Protein Interaction Domains and Motifs
  • Recombinant Proteins
  • Sulfur / chemistry*
  • Sulfur / metabolism

Substances

  • Iron-Sulfur Proteins
  • Recombinant Proteins
  • Sulfur
  • Iron
  • Carbon-Sulfur Lyases
  • cysteine desulfurase
  • Cysteine