Translocation of α-synuclein expressed in Escherichia coli
Translocation of α-synuclein expressed in Escherichia coli
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DOI：
10.1128/jb.01406-06
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发表时间：
2007-04-01
影响因子：
3.2
通讯作者：
Wang, Chih-chen
中科院分区：
文献类型：
--
作者：
Ren, Guoping;Wang, Xi;Wang, Chih-chen
α-突触核蛋白是帕金森病路易氏小体的主要成分。虽然没有明显的信号序列，但在大肠杆菌中表达的α-突触核蛋白主要位于周质中。排除了α-突触核蛋白通过细菌中鉴定的SECA或TAT靶向途径穿过内膜进入周质，以及通过MSCL释放α-突触核蛋白的可能性。α-突触核蛋白的转位与信号识别颗粒依赖的途径有关。α-突触核蛋白分子的C-末端99-140部分与中央的61-95部分协同作用，为其移位到周质中发挥了信号样作用。这种易位不需要N-末端1-60区域。
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.