Abstract
In this study, a naturally unsecretory intrinsically disordered domain of nucleoskeletal-like protein (Nsp) was attempted to be secreted with different types of secretion signals in Bacillus subtilis. The results showed that Nsp can be secreted efficiently by all selected Sec-type signal peptides. Nsp was successfully exported when fused to Tat-type signal peptides but less efficient than Sec-type. The fusion protein with the non-classical extracellular proteins can be detected in the cell and extracellular milieu. This study further demonstrated that the mature protein plays an important role in protein secretion. Moreover, these results indicated that Nsp could be a useful tool to understand the individual roles of mature proteins and signal peptide in protein secretion, to evaluate the effect of conformation of mature proteins on their export pathway when coupled with Tat-type signal peptide, and to seek the signal of non-classical secretory proteins.
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Acknowledgments
We thank Hamid Majeed for critical review of this manuscript. This work was supported by the National Science Fund for Distinguished Young Scholars (31125021), the National High Technology Research and Development Program of China (2011AA100905), the National Natural Science Foundation of China (No. 31171636), the Key program of National Natural Science Foundation of China (No. 20836003), the National Basic Research Program of China 973 Program (2012CB720802), the 111 project B07029, and SKLF-TS-201101.
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Wang, G., Chen, H., Zhang, H. et al. The Secretion of an Intrinsically Disordered Protein with Different Secretion Signals in Bacillus subtilis . Curr Microbiol 66, 566–572 (2013). https://doi.org/10.1007/s00284-013-0315-8
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DOI: https://doi.org/10.1007/s00284-013-0315-8