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

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
586
Issue
19
Identifiers
DOI: 10.1016/j.febslet.2012.08.002
Keywords
  • Sulfiredoxin
  • Dna Binding
  • Ca2+-Dependent Nuclease Activity
Disciplines
  • Biology

Abstract

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.

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