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拟南芥硫氧还蛋白的双重功能:作为一种依赖于氧化还原的亚磺酸还原酶和一种不依赖于氧化还原的核酸内切酶。

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

机构信息

Division of Applied Life Science (BK21 Program) and PMBBRC, Gyeongsang National University, Jinju, Republic of Korea.

出版信息

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.

摘要

基于已知的作为一种依赖于氧化还原的亚磺酸还原酶的硫氧还蛋白(Srx)的氨基酸序列与核酸酶 ParB 具有高度序列同源性这一事实,我们检测了拟南芥(AtSrx)中重组 Srx 的核酸结合和水解活性。我们发现 AtSrx 作为一种核酸酶,能够以单链和双链 DNA 作为底物。该核酸酶活性可被二价阳离子增强。特别是,通过定点突变亚磺酸还原酶的活性位点半胱氨酸(Cys72)为丝氨酸(AtSrx-C72S),我们证明了 AtSrx 的还原酶活性的活性位点不参与其核酸酶功能。

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