State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, People's Republic of China.
Curr Microbiol. 2013 Jun;66(6):566-72. doi: 10.1007/s00284-013-0315-8. Epub 2013 Jan 29.
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.
在这项研究中，我们尝试使用不同类型的分泌信号在枯草芽孢杆菌中分泌核骨架样蛋白（Nsp）的天然无分泌结构域。结果表明，Nsp 可以被所有选定的 Sec 型信号肽有效地分泌。当融合到 Tat 型信号肽时，Nsp 也能成功输出，但效率低于 Sec 型。带有非经典细胞外蛋白的融合蛋白可以在细胞和细胞外环境中检测到。本研究进一步证明成熟蛋白在蛋白分泌中起着重要作用。此外，这些结果表明，Nsp 可以成为一种有用的工具，用于理解成熟蛋白和信号肽在蛋白分泌中的单独作用，评估当与 Tat 型信号肽偶联时成熟蛋白构象对其输出途径的影响，并寻找非经典分泌蛋白的信号。
