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J. Bacteriol. doi:10.1128/JB.01406-06
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

TRANSLOCATION OF -SYNUCLEIN EXPRESSED IN ESCHERICHIA COLI

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China, Graduate School of the Chinese Academy of Sciences, China, Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China

^* To whom correspondence should be addressed. Email: chihwang{at}sun5.ibp.ac.cn.

	Abstract

á-Synuclein is a major component of Lewy bodies in Parkinson's disease. Although no signal sequence is apparent, á-synuclein expressed in Escherichia coli is mostly located in the periplasm. The possibilities, that á-synuclein translocated into the periplasm across the inner membrane by the SecA or the Tat targeting route identified in bacteria, and that á-synuclein was released through MscL, were excluded. The SRP-dependent pathway is involved in the translocation of á-synuclein. The C-terminal 99-140 portion of the á-synuclein molecule plays a signal-like role for its translocation into the periplasm, cooperating with the central 61-95 section. The N-terminal 1-60 region is not required for the translocation.

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