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.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Arabidopsis / genetics
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Arabidopsis / metabolism*
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Arabidopsis Proteins / genetics
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Arabidopsis Proteins / metabolism*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Base Sequence
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Cations, Divalent / pharmacology
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DNA, Plant / genetics
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Deoxyribonucleases / genetics
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Deoxyribonucleases / metabolism
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Molecular Sequence Data
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Oxidation-Reduction
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Oxidoreductases Acting on Sulfur Group Donors / genetics
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Oxidoreductases Acting on Sulfur Group Donors / metabolism*
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Reactive Oxygen Species / metabolism
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Sulfinic Acids / metabolism
Substances
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Arabidopsis Proteins
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Bacterial Proteins
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Cations, Divalent
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DNA, Plant
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Reactive Oxygen Species
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Recombinant Proteins
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Sulfinic Acids
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Oxidoreductases Acting on Sulfur Group Donors
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sulfiredoxin protein, Arabidopsis
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Deoxyribonucleases