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J. Biol. Chem., Vol. 280, Issue 29, 27029-27034, July 22, 2005

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Periplasmic Protein HdeA Exhibits Chaperone-like Activity Exclusively within Stomach pH Range by Transforming into Disordered Conformation^*

Weizhe Hong¶, Wangwang Jiao¶, Jicheng Hu||, Junrui Zhang, Chong Liu¶, Xinmiao Fu, Dan Shen¶, Bin Xia||**, and Zengyi Chang

From the The National Laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences and ^**College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, ^¶Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, and ^||Beijing Nuclear Magnetic Resonance Center, Beijing 100871, China

The extremely acidic environment of the mammalian stomach, with a pH range usually between 1 and 3, represents a stressful challenge for enteric pathogenic bacteria such as Escherichia coli before they enter into the intestine. The hdeA gene of E. coli was found to be acid inducible and was revealed by genetic studies to be important for the acid survival of the strain. This study was performed in an attempt to characterize the mechanism of the activity of the HdeA protein. Our data provided in this report strongly suggest that HdeA employs a novel strategy to modulate its chaperone activity: it possesses an ordered conformation that is unable to bind denatured substrate proteins under normal physiological conditions (i.e. at neutral pH) and transforms into a globally disordered conformation that is able to bind substrate proteins under stress conditions (i.e. at a pH below 3). Furthermore, our data indicate that HdeA exposes hydrophobic surfaces that appear to be involved in the binding of denatured substrate proteins at extremely low pH values. In light of our observations, models are proposed to explain the action of HdeA in both a physiological and a molecular context.

Received for publication, April 12, 2005 , and in revised form, May 16, 2005.

^* This work was supported in part by Grant 30270289 from the National Natural Science Foundation of China, Grant G1999075607 from the National Key Basic Research Foundation of China, Grant G39725008 from the National Science Foundation for Outstanding Young Scientists in China (to Z. C.), and Grant 30125009 from the National Natural Science Foundation of China (to B. X.). 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.

To whom correspondence should be addressed. Tel.: 86-10-6275-8822; Fax: 86-10-6275-1526; E-mail: changzy{at}pku.edu.cn.

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