A Novel Signal Peptide Derived from Bacillus Licheniformis α-Amylase Efficiently Targets Recombinant Human Activin A to the Periplasm of Escherichia coli

Journal of Cell and Molecular Research

مقاله 1، دوره 10، شماره 1 - شماره پیاپی 19، آذر 2018، صفحه 47-51   

نوع مقاله: Scientific Reports

شناسه دیجیتال (DOI): 10.22067/jcmr.v8i2.64629

نویسندگان

Zahra Hajihassan^{* 1}؛ Seyed kazem Hosseini¹؛ Alireza Zomorodipour²

¹University of Tehran

²National institute of Genetic Engineering and Biotechnology

چکیده

Human activin A is a member of the transforming growth factor-β superfamily consists of two similar beta subunits. Activin A is expressed by different cells and displays numerous biological activities such as control of neuronal cell proliferation and differentiation, promotion of neuronal survival in the body. Therefore, recombinant production of activin A is beneficial because it can be used to treat many neurodegenerative diseases such as Alzheimer's and Parkinson diseases. In this study E. coli as a cheap and fast-growing host was selected to produce recombinant human activin A. As cytoplasmic expression of human activin A with complex structure and disulfide bonds produces inclusion bodies, so periplasmic expression of it can be beneficial. Therefore, we used modified Iranian B. licheniformis α-amylase signal peptide as a new signal peptide in order to translocate the recombinant activin A through the inner membrane. In this study human pro-activin A cDNA and signal sequence were cloned in pET21b vector and resulting vector transformed into the two strains of E. coli BL21. SDS-PAGE and western blot techniques were used to confirm recombinant activin A expression. Finally, our results indicated that the signal peptide used in this study was effective for secretion of activin A into the periplasmic space of E. coli.

کلیدواژه‌ها

Activin A؛ modified α-amylase signal peptide؛ periplasmic expression

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