Current Microbiology

, Volume 66, Issue 6, pp 566–572

The Secretion of an Intrinsically Disordered Protein with Different Secretion Signals in Bacillus subtilis

Authors

  • Guangqiang Wang
    • State Key Laboratory of Food Science and TechnologyJiangnan University
  • Haiqin Chen
    • School of Food Science and TechnologyJiangnan University
  • Hao Zhang
    • School of Food Science and TechnologyJiangnan University
    • School of Food Science and TechnologyJiangnan University
    • School of Food Science and TechnologyJiangnan University
Article

DOI: 10.1007/s00284-013-0315-8

Cite this article as:
Wang, G., Chen, H., Zhang, H. et al. Curr Microbiol (2013) 66: 566. doi:10.1007/s00284-013-0315-8

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.

Supplementary material

284_2013_315_MOESM1_ESM.pdf (96 kb)
Supplementary material 1 (PDF 95 kb)

Copyright information

© Springer Science+Business Media New York 2013