Translocation of α-Synuclein Expressed in Escherichia coli
Author(s) -
Guoping Ren,
Xi Wang,
Shufeng Hao,
HongYu Hu,
Chih-chen Wang
Publication year - 2007
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.01406-06
Subject(s) - periplasmic space , biology , chromosomal translocation , escherichia coli , signal peptide , twin arginine translocation pathway , bacterial outer membrane , signal recognition particle , microbiology and biotechnology , biochemistry , peptide sequence , gene
alpha-Synuclein is a major component of Lewy bodies in Parkinson's disease. Although no signal sequence is apparent, alpha-synuclein expressed in Escherichia coli is mostly located in the periplasm. The possibilities that alpha-synuclein translocated into the periplasm across the inner membrane by the SecA or the Tat targeting route identified in bacteria and that alpha-synuclein was released through MscL were excluded. The signal recognition particle-dependent pathway is involved in the translocation of alpha-synuclein. The C-terminal 99-to-140 portion of the alpha-synuclein molecule plays a signal-like role for its translocation into the periplasm, cooperating with the central 61-to-95 section. The N-terminal 1-to-60 region is not required for this translocation.
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