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J. Biol. Chem., Vol. 278, Issue 45, 44552-44559, November 7, 2003
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**
From the
Beamline Division, Pohang Accelerator Laboratory, Pohang, 790-784, Department of Life Science, Pohang University of Science and Technology, Pohang, 790-784, ¶Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul, 151-742, and ||National Creative Research Initiative Center for Behavioral Genetics, Department of Biological Science, Korea Advanced Institute of Science and Technology, Taejon, 305-710, Republic of Korea
Human DJ-1 and Escherichia coli Hsp31 belong to ThiJ/PfpI family, whose members contain a conserved domain. DJ-1 is associated with autosomal recessive early onset parkinsonism and Hsp31 is a molecular chaperone. Structural comparisons between DJ-1, Hsp31, and an Archaea protease, a member of ThiJ/PfpI family, lead to the identification of the chaperone activity of DJ-1 and the proteolytic activity of Hsp31. Moreover, the comparisons provide insights into how the functional diversity is realized in proteins that share an evolutionarily conserved domain. On the basis of the chaperone activity the possible role of DJ-1 in the pathogenesis of Parkinson's disease is discussed.
Received for publication, April 30, 2003 , and in revised form, August 18, 2003.
The atomic coordinates and structure factors (code 1IZY
* This study was supported by a grant from the Korea Health 21 R&D Project, Ministry of Health and Welfare and in part by grants from The Center for Biological Modulators. 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: Beamline Division, Pohang Accelerator Laboratory, Pohang, 790-784, Kyungbuk, Republic of Korea. Tel.: 82-54-279-1563; Fax: 82-54-279-1598; E-mail: chajung{at}postech.ac.kr.
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