Dual functions of Arabidopsis sulfiredoxin: acting as a redox-dependent sulfinic acid reductase and as a redox-independent nuclease enzyme

FEBS Lett. 2012 Sep 21;586(19):3493-9. doi: 10.1016/j.febslet.2012.08.002. Epub 2012 Aug 10.

Abstract

Based on the fact that the amino acid sequence of sulfiredoxin (Srx), already known as a redox-dependent sulfinic acid reductase, showed a high sequence homology with that of ParB, a nuclease enzyme, we examined the nucleic acid binding and hydrolyzing activity of the recombinant Srx in Arabidopsis (AtSrx). We found that AtSrx functions as a nuclease enzyme that can use single-stranded and double-stranded DNAs as substrates. The nuclease activity was enhanced by divalent cations. Particularly, by point-mutating the active site of sulfinate reductase, Cys (72) to Ser (AtSrx-C72S), we demonstrate that the active site of the reductase function of AtSrx is not involved in its nuclease function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / genetics
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Cations, Divalent / pharmacology
  • DNA, Plant / genetics
  • Deoxyribonucleases / genetics
  • Deoxyribonucleases / metabolism
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Oxidoreductases Acting on Sulfur Group Donors / genetics
  • Oxidoreductases Acting on Sulfur Group Donors / metabolism*
  • Reactive Oxygen Species / metabolism
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Sulfinic Acids / metabolism

Substances

  • Arabidopsis Proteins
  • Bacterial Proteins
  • Cations, Divalent
  • DNA, Plant
  • Reactive Oxygen Species
  • Recombinant Proteins
  • Sulfinic Acids
  • Oxidoreductases Acting on Sulfur Group Donors
  • sulfiredoxin protein, Arabidopsis
  • Deoxyribonucleases