ArticleCurrent microbiology2013
The secretion of an intrinsically disordered protein with different secretion signals in Bacillus subtilis.
Article in Current microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- NonClasGP-Pred: robust and efficient prediction of non-classically secreted proteins by integrating subset-specific optimal models of imbalanced data.Microbial genomics · 2020Article
- The YoaW signal peptide directs efficient secretion of different heterologous proteins fused to a StrepII-SUMO tag in Bacillus subtilis.Microbial cell factories · 2019Article
- Use of a Novel Report Protein to Study the Secretion Signal of Flagellin in Bacillus subtilis.Current microbiology · 2016Article
- A novel strategy for protein production using non-classical secretion pathway in Bacillus subtilis.Microbial cell factories · 2016Article
- Common Non-classically Secreted Bacterial Proteins with Experimental Evidence.Current microbiology · 2016Review
- Article
- A new potential secretion pathway for recombinant proteins in Bacillus subtilis.Microbial cell factories · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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Registered trials
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