Identification and characterization of single-domain thiosulfate sulfurtransferases from Arabidopsis thaliana

FEBS Lett. 2002 Dec 18;532(3):427-31. doi: 10.1016/s0014-5793(02)03723-7.

Abstract

Sulfurtransferases/rhodaneses (ST) are a group of enzymes widely distributed in all three phyla that catalyze the transfer of sulfur from a donor to a thiophilic acceptor substrate. All ST contain distinct structural domains, and can exist as single-domain proteins, as tandemly repeated modules in which the C-terminal domain bears the active site, or as members of multi-domain proteins. We identified several ST in Arabidopsis resembling the C-terminus of the Arabidopsis two-domain ST1 and the single-domain GlpE protein from Escherichia coli. Two of them (accession numbers BAB10422 and BAB10409) were expressed in E. coli and purified. Both proteins showed thiosulfate-specific ST enzyme activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / enzymology*
  • Catalytic Domain
  • Cloning, Molecular
  • DNA, Complementary / metabolism
  • DNA-Binding Proteins / chemistry*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins*
  • Kinetics
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid

Substances

  • DNA, Complementary
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • GlpE protein, E coli