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J. Biol. Chem., Vol. 281, Issue 12, 8296-8304, March 24, 2006

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The Bacillus subtilis YkuV Is a Thiol:Disulfide Oxidoreductase Revealed by Its Redox Structures and Activity^*

Xinxin Zhang, Yunfei Hu, Xianrong Guo^¶, Ewen Lescop, You Li^¶, Bin Xia^¶, and Changwen Jin^¶1

From the Beijing Nuclear Magnetic Resonance Center, College of Life Sciences, and ^¶College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China

The Bacillus subtilis YkuV responds to environmental oxidative stress and plays an important role for the bacteria to adapt to the environment. Bioinformatic analysis suggests that YkuV is a homolog of membrane-anchored proteins and belongs to the thioredoxin-like protein superfamily containing the typical Cys-Xaa-Xaa-Cys active motif. However, the biological function of this protein remains unknown thus far. In order to elucidate the biological function, we have determined the solution structures of both the oxidized and reduced forms of B. subtilis YkuV by NMR spectroscopy and performed biochemical studies. Our results demonstrated that the reduced YkuV has a low midpoint redox potential, allowing it to reduce a variety of protein substrates. The overall structures of both oxidized and reduced forms are similar, with a typical thioredoxin-like fold. However, significant conformational changes in the Cys-Xaa-Xaa-Cys active motif of the tertiary structures are observed between the two forms. In addition, the backbone dynamics provide further insights in understanding the strong redox potential of the reduced YkuV. Furthermore, we demonstrated that YkuV is able to reduce different protein substrates in vitro. Together, our results clearly established that YkuV may function as a general thiol:disulfide oxidoreductase, which acts as an alternative for thioredoxin or thioredoxin reductase to maintain the reducing environment in the cell cytoplasm.

Received for publication, November 8, 2005 , and in revised form, January 6, 2006.

The atomic coordinates and structure factors (codes 2B5X and 2B5Y) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the National Natural Science Foundation of China Grant 30125009 (to B. X.) and Grant 30325010 (to C. J.).The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing 100871, China. Tel.: 86-10-6275-6004; Fax: 86-10-6275-3790; E-mail: changwen{at}pku.edu.cn.

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